qx 222  (Alomone Labs)


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    Structured Review

    Alomone Labs qx 222
    Structure of the external access pathway. The proposed molecular arrangement of crucial amino acids involved in access and binding of <t>QX-222</t> is shown. A and B ), respectively, based
    Qx 222, supplied by Alomone Labs, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/qx 222/product/Alomone Labs
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    qx 222 - by Bioz Stars, 2022-07
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    Images

    1) Product Images from "Exploring the Structure of the Voltage-gated Na+ Channel by an Engineered Drug Access Pathway to the Receptor Site for Local Anesthetics *"

    Article Title: Exploring the Structure of the Voltage-gated Na+ Channel by an Engineered Drug Access Pathway to the Receptor Site for Local Anesthetics *

    Journal: The Journal of Biological Chemistry

    doi: 10.1074/jbc.M113.541763

    Structure of the external access pathway. The proposed molecular arrangement of crucial amino acids involved in access and binding of QX-222 is shown. A and B ), respectively, based
    Figure Legend Snippet: Structure of the external access pathway. The proposed molecular arrangement of crucial amino acids involved in access and binding of QX-222 is shown. A and B ), respectively, based

    Techniques Used: Binding Assay

    Recovery from block by intracellular QX-222. A 5-s-long 10-Hz pulse train was applied for repetitive openings of the channels to bind QX-222 to the inner vestibule. After the last pulse in the train, the cell was repolarized to −140 mV for various
    Figure Legend Snippet: Recovery from block by intracellular QX-222. A 5-s-long 10-Hz pulse train was applied for repetitive openings of the channels to bind QX-222 to the inner vestibule. After the last pulse in the train, the cell was repolarized to −140 mV for various

    Techniques Used: Blocking Assay

    The binding site for external QX-222 is in the internal vestibule. Modulation of the EAP by an additional mutation in the selectivity filter and by mutations of Trp-1531 is shown. The stimulation protocol and depiction are the same as in B. A , residue
    Figure Legend Snippet: The binding site for external QX-222 is in the internal vestibule. Modulation of the EAP by an additional mutation in the selectivity filter and by mutations of Trp-1531 is shown. The stimulation protocol and depiction are the same as in B. A , residue

    Techniques Used: Binding Assay, Mutagenesis

    Mutations at Site 1575 Open an EAP for QX-222
    Figure Legend Snippet: Mutations at Site 1575 Open an EAP for QX-222

    Techniques Used:

    Effect of QX-222 on inactivation properties of channels carrying mutations at site 1531. A , in W1531A, 500 μ m QX-222 significantly shifted the steady-state inactivation curve to hyperpolarized potentials. V 1/2 was −74.6 ± 0.6 and
    Figure Legend Snippet: Effect of QX-222 on inactivation properties of channels carrying mutations at site 1531. A , in W1531A, 500 μ m QX-222 significantly shifted the steady-state inactivation curve to hyperpolarized potentials. V 1/2 was −74.6 ± 0.6 and

    Techniques Used:

    External block by QX-222 is favored by replacement of Ile-1575 with amino acids of small size or with hydrophilic properties. Sodium currents were evoked by depolarizing pulses at a frequency of 2 Hz (see “Experimental Procedures”). Connecting
    Figure Legend Snippet: External block by QX-222 is favored by replacement of Ile-1575 with amino acids of small size or with hydrophilic properties. Sodium currents were evoked by depolarizing pulses at a frequency of 2 Hz (see “Experimental Procedures”). Connecting

    Techniques Used: Blocking Assay

    Use-dependent block by external QX-222. A 2-Hz pulse train was applied for 30 s at a holding potential of −120 mV. Thereafter, external perfusion with QX-222 was started while cells were kept at the holding potential for 120 s. Then repetitive
    Figure Legend Snippet: Use-dependent block by external QX-222. A 2-Hz pulse train was applied for 30 s at a holding potential of −120 mV. Thereafter, external perfusion with QX-222 was started while cells were kept at the holding potential for 120 s. Then repetitive

    Techniques Used: Blocking Assay

    2) Product Images from "Exploring the Structure of the Voltage-gated Na+ Channel by an Engineered Drug Access Pathway to the Receptor Site for Local Anesthetics *"

    Article Title: Exploring the Structure of the Voltage-gated Na+ Channel by an Engineered Drug Access Pathway to the Receptor Site for Local Anesthetics *

    Journal: The Journal of Biological Chemistry

    doi: 10.1074/jbc.M113.541763

    Structure of the external access pathway. The proposed molecular arrangement of crucial amino acids involved in access and binding of QX-222 is shown. A and B ), respectively, based
    Figure Legend Snippet: Structure of the external access pathway. The proposed molecular arrangement of crucial amino acids involved in access and binding of QX-222 is shown. A and B ), respectively, based

    Techniques Used: Binding Assay

    Recovery from block by intracellular QX-222. A 5-s-long 10-Hz pulse train was applied for repetitive openings of the channels to bind QX-222 to the inner vestibule. After the last pulse in the train, the cell was repolarized to −140 mV for various
    Figure Legend Snippet: Recovery from block by intracellular QX-222. A 5-s-long 10-Hz pulse train was applied for repetitive openings of the channels to bind QX-222 to the inner vestibule. After the last pulse in the train, the cell was repolarized to −140 mV for various

    Techniques Used: Blocking Assay

    The binding site for external QX-222 is in the internal vestibule. Modulation of the EAP by an additional mutation in the selectivity filter and by mutations of Trp-1531 is shown. The stimulation protocol and depiction are the same as in B. A , residue
    Figure Legend Snippet: The binding site for external QX-222 is in the internal vestibule. Modulation of the EAP by an additional mutation in the selectivity filter and by mutations of Trp-1531 is shown. The stimulation protocol and depiction are the same as in B. A , residue

    Techniques Used: Binding Assay, Mutagenesis

    Mutations at Site 1575 Open an EAP for QX-222
    Figure Legend Snippet: Mutations at Site 1575 Open an EAP for QX-222

    Techniques Used:

    Effect of QX-222 on inactivation properties of channels carrying mutations at site 1531. A , in W1531A, 500 μ m QX-222 significantly shifted the steady-state inactivation curve to hyperpolarized potentials. V 1/2 was −74.6 ± 0.6 and
    Figure Legend Snippet: Effect of QX-222 on inactivation properties of channels carrying mutations at site 1531. A , in W1531A, 500 μ m QX-222 significantly shifted the steady-state inactivation curve to hyperpolarized potentials. V 1/2 was −74.6 ± 0.6 and

    Techniques Used:

    External block by QX-222 is favored by replacement of Ile-1575 with amino acids of small size or with hydrophilic properties. Sodium currents were evoked by depolarizing pulses at a frequency of 2 Hz (see “Experimental Procedures”). Connecting
    Figure Legend Snippet: External block by QX-222 is favored by replacement of Ile-1575 with amino acids of small size or with hydrophilic properties. Sodium currents were evoked by depolarizing pulses at a frequency of 2 Hz (see “Experimental Procedures”). Connecting

    Techniques Used: Blocking Assay

    Use-dependent block by external QX-222. A 2-Hz pulse train was applied for 30 s at a holding potential of −120 mV. Thereafter, external perfusion with QX-222 was started while cells were kept at the holding potential for 120 s. Then repetitive
    Figure Legend Snippet: Use-dependent block by external QX-222. A 2-Hz pulse train was applied for 30 s at a holding potential of −120 mV. Thereafter, external perfusion with QX-222 was started while cells were kept at the holding potential for 120 s. Then repetitive

    Techniques Used: Blocking Assay

    3) Product Images from "Exploring the Structure of the Voltage-gated Na+ Channel by an Engineered Drug Access Pathway to the Receptor Site for Local Anesthetics *"

    Article Title: Exploring the Structure of the Voltage-gated Na+ Channel by an Engineered Drug Access Pathway to the Receptor Site for Local Anesthetics *

    Journal: The Journal of Biological Chemistry

    doi: 10.1074/jbc.M113.541763

    Structure of the external access pathway. The proposed molecular arrangement of crucial amino acids involved in access and binding of QX-222 is shown. A and B ), respectively, based
    Figure Legend Snippet: Structure of the external access pathway. The proposed molecular arrangement of crucial amino acids involved in access and binding of QX-222 is shown. A and B ), respectively, based

    Techniques Used: Binding Assay

    Recovery from block by intracellular QX-222. A 5-s-long 10-Hz pulse train was applied for repetitive openings of the channels to bind QX-222 to the inner vestibule. After the last pulse in the train, the cell was repolarized to −140 mV for various
    Figure Legend Snippet: Recovery from block by intracellular QX-222. A 5-s-long 10-Hz pulse train was applied for repetitive openings of the channels to bind QX-222 to the inner vestibule. After the last pulse in the train, the cell was repolarized to −140 mV for various

    Techniques Used: Blocking Assay

    The binding site for external QX-222 is in the internal vestibule. Modulation of the EAP by an additional mutation in the selectivity filter and by mutations of Trp-1531 is shown. The stimulation protocol and depiction are the same as in B. A , residue
    Figure Legend Snippet: The binding site for external QX-222 is in the internal vestibule. Modulation of the EAP by an additional mutation in the selectivity filter and by mutations of Trp-1531 is shown. The stimulation protocol and depiction are the same as in B. A , residue

    Techniques Used: Binding Assay, Mutagenesis

    Mutations at Site 1575 Open an EAP for QX-222
    Figure Legend Snippet: Mutations at Site 1575 Open an EAP for QX-222

    Techniques Used:

    Effect of QX-222 on inactivation properties of channels carrying mutations at site 1531. A , in W1531A, 500 μ m QX-222 significantly shifted the steady-state inactivation curve to hyperpolarized potentials. V 1/2 was −74.6 ± 0.6 and
    Figure Legend Snippet: Effect of QX-222 on inactivation properties of channels carrying mutations at site 1531. A , in W1531A, 500 μ m QX-222 significantly shifted the steady-state inactivation curve to hyperpolarized potentials. V 1/2 was −74.6 ± 0.6 and

    Techniques Used:

    External block by QX-222 is favored by replacement of Ile-1575 with amino acids of small size or with hydrophilic properties. Sodium currents were evoked by depolarizing pulses at a frequency of 2 Hz (see “Experimental Procedures”). Connecting
    Figure Legend Snippet: External block by QX-222 is favored by replacement of Ile-1575 with amino acids of small size or with hydrophilic properties. Sodium currents were evoked by depolarizing pulses at a frequency of 2 Hz (see “Experimental Procedures”). Connecting

    Techniques Used: Blocking Assay

    Use-dependent block by external QX-222. A 2-Hz pulse train was applied for 30 s at a holding potential of −120 mV. Thereafter, external perfusion with QX-222 was started while cells were kept at the holding potential for 120 s. Then repetitive
    Figure Legend Snippet: Use-dependent block by external QX-222. A 2-Hz pulse train was applied for 30 s at a holding potential of −120 mV. Thereafter, external perfusion with QX-222 was started while cells were kept at the holding potential for 120 s. Then repetitive

    Techniques Used: Blocking Assay

    4) Product Images from "Exploring the Structure of the Voltage-gated Na+ Channel by an Engineered Drug Access Pathway to the Receptor Site for Local Anesthetics *"

    Article Title: Exploring the Structure of the Voltage-gated Na+ Channel by an Engineered Drug Access Pathway to the Receptor Site for Local Anesthetics *

    Journal: The Journal of Biological Chemistry

    doi: 10.1074/jbc.M113.541763

    Structure of the external access pathway. The proposed molecular arrangement of crucial amino acids involved in access and binding of QX-222 is shown. A and B ), respectively, based
    Figure Legend Snippet: Structure of the external access pathway. The proposed molecular arrangement of crucial amino acids involved in access and binding of QX-222 is shown. A and B ), respectively, based

    Techniques Used: Binding Assay

    Recovery from block by intracellular QX-222. A 5-s-long 10-Hz pulse train was applied for repetitive openings of the channels to bind QX-222 to the inner vestibule. After the last pulse in the train, the cell was repolarized to −140 mV for various
    Figure Legend Snippet: Recovery from block by intracellular QX-222. A 5-s-long 10-Hz pulse train was applied for repetitive openings of the channels to bind QX-222 to the inner vestibule. After the last pulse in the train, the cell was repolarized to −140 mV for various

    Techniques Used: Blocking Assay

    The binding site for external QX-222 is in the internal vestibule. Modulation of the EAP by an additional mutation in the selectivity filter and by mutations of Trp-1531 is shown. The stimulation protocol and depiction are the same as in B. A , residue
    Figure Legend Snippet: The binding site for external QX-222 is in the internal vestibule. Modulation of the EAP by an additional mutation in the selectivity filter and by mutations of Trp-1531 is shown. The stimulation protocol and depiction are the same as in B. A , residue

    Techniques Used: Binding Assay, Mutagenesis

    Mutations at Site 1575 Open an EAP for QX-222
    Figure Legend Snippet: Mutations at Site 1575 Open an EAP for QX-222

    Techniques Used:

    Effect of QX-222 on inactivation properties of channels carrying mutations at site 1531. A , in W1531A, 500 μ m QX-222 significantly shifted the steady-state inactivation curve to hyperpolarized potentials. V 1/2 was −74.6 ± 0.6 and
    Figure Legend Snippet: Effect of QX-222 on inactivation properties of channels carrying mutations at site 1531. A , in W1531A, 500 μ m QX-222 significantly shifted the steady-state inactivation curve to hyperpolarized potentials. V 1/2 was −74.6 ± 0.6 and

    Techniques Used:

    External block by QX-222 is favored by replacement of Ile-1575 with amino acids of small size or with hydrophilic properties. Sodium currents were evoked by depolarizing pulses at a frequency of 2 Hz (see “Experimental Procedures”). Connecting
    Figure Legend Snippet: External block by QX-222 is favored by replacement of Ile-1575 with amino acids of small size or with hydrophilic properties. Sodium currents were evoked by depolarizing pulses at a frequency of 2 Hz (see “Experimental Procedures”). Connecting

    Techniques Used: Blocking Assay

    Use-dependent block by external QX-222. A 2-Hz pulse train was applied for 30 s at a holding potential of −120 mV. Thereafter, external perfusion with QX-222 was started while cells were kept at the holding potential for 120 s. Then repetitive
    Figure Legend Snippet: Use-dependent block by external QX-222. A 2-Hz pulse train was applied for 30 s at a holding potential of −120 mV. Thereafter, external perfusion with QX-222 was started while cells were kept at the holding potential for 120 s. Then repetitive

    Techniques Used: Blocking Assay

    5) Product Images from "Exploring the Structure of the Voltage-gated Na+ Channel by an Engineered Drug Access Pathway to the Receptor Site for Local Anesthetics *"

    Article Title: Exploring the Structure of the Voltage-gated Na+ Channel by an Engineered Drug Access Pathway to the Receptor Site for Local Anesthetics *

    Journal: The Journal of Biological Chemistry

    doi: 10.1074/jbc.M113.541763

    Structure of the external access pathway. The proposed molecular arrangement of crucial amino acids involved in access and binding of QX-222 is shown. A and B ), respectively, based
    Figure Legend Snippet: Structure of the external access pathway. The proposed molecular arrangement of crucial amino acids involved in access and binding of QX-222 is shown. A and B ), respectively, based

    Techniques Used: Binding Assay

    Recovery from block by intracellular QX-222. A 5-s-long 10-Hz pulse train was applied for repetitive openings of the channels to bind QX-222 to the inner vestibule. After the last pulse in the train, the cell was repolarized to −140 mV for various
    Figure Legend Snippet: Recovery from block by intracellular QX-222. A 5-s-long 10-Hz pulse train was applied for repetitive openings of the channels to bind QX-222 to the inner vestibule. After the last pulse in the train, the cell was repolarized to −140 mV for various

    Techniques Used: Blocking Assay

    The binding site for external QX-222 is in the internal vestibule. Modulation of the EAP by an additional mutation in the selectivity filter and by mutations of Trp-1531 is shown. The stimulation protocol and depiction are the same as in B. A , residue
    Figure Legend Snippet: The binding site for external QX-222 is in the internal vestibule. Modulation of the EAP by an additional mutation in the selectivity filter and by mutations of Trp-1531 is shown. The stimulation protocol and depiction are the same as in B. A , residue

    Techniques Used: Binding Assay, Mutagenesis

    Mutations at Site 1575 Open an EAP for QX-222
    Figure Legend Snippet: Mutations at Site 1575 Open an EAP for QX-222

    Techniques Used:

    Effect of QX-222 on inactivation properties of channels carrying mutations at site 1531. A , in W1531A, 500 μ m QX-222 significantly shifted the steady-state inactivation curve to hyperpolarized potentials. V 1/2 was −74.6 ± 0.6 and
    Figure Legend Snippet: Effect of QX-222 on inactivation properties of channels carrying mutations at site 1531. A , in W1531A, 500 μ m QX-222 significantly shifted the steady-state inactivation curve to hyperpolarized potentials. V 1/2 was −74.6 ± 0.6 and

    Techniques Used:

    External block by QX-222 is favored by replacement of Ile-1575 with amino acids of small size or with hydrophilic properties. Sodium currents were evoked by depolarizing pulses at a frequency of 2 Hz (see “Experimental Procedures”). Connecting
    Figure Legend Snippet: External block by QX-222 is favored by replacement of Ile-1575 with amino acids of small size or with hydrophilic properties. Sodium currents were evoked by depolarizing pulses at a frequency of 2 Hz (see “Experimental Procedures”). Connecting

    Techniques Used: Blocking Assay

    Use-dependent block by external QX-222. A 2-Hz pulse train was applied for 30 s at a holding potential of −120 mV. Thereafter, external perfusion with QX-222 was started while cells were kept at the holding potential for 120 s. Then repetitive
    Figure Legend Snippet: Use-dependent block by external QX-222. A 2-Hz pulse train was applied for 30 s at a holding potential of −120 mV. Thereafter, external perfusion with QX-222 was started while cells were kept at the holding potential for 120 s. Then repetitive

    Techniques Used: Blocking Assay

    6) Product Images from "Exploring the Structure of the Voltage-gated Na+ Channel by an Engineered Drug Access Pathway to the Receptor Site for Local Anesthetics *"

    Article Title: Exploring the Structure of the Voltage-gated Na+ Channel by an Engineered Drug Access Pathway to the Receptor Site for Local Anesthetics *

    Journal: The Journal of Biological Chemistry

    doi: 10.1074/jbc.M113.541763

    Structure of the external access pathway. The proposed molecular arrangement of crucial amino acids involved in access and binding of QX-222 is shown. A and B ), respectively, based
    Figure Legend Snippet: Structure of the external access pathway. The proposed molecular arrangement of crucial amino acids involved in access and binding of QX-222 is shown. A and B ), respectively, based

    Techniques Used: Binding Assay

    Recovery from block by intracellular QX-222. A 5-s-long 10-Hz pulse train was applied for repetitive openings of the channels to bind QX-222 to the inner vestibule. After the last pulse in the train, the cell was repolarized to −140 mV for various
    Figure Legend Snippet: Recovery from block by intracellular QX-222. A 5-s-long 10-Hz pulse train was applied for repetitive openings of the channels to bind QX-222 to the inner vestibule. After the last pulse in the train, the cell was repolarized to −140 mV for various

    Techniques Used: Blocking Assay

    The binding site for external QX-222 is in the internal vestibule. Modulation of the EAP by an additional mutation in the selectivity filter and by mutations of Trp-1531 is shown. The stimulation protocol and depiction are the same as in B. A , residue
    Figure Legend Snippet: The binding site for external QX-222 is in the internal vestibule. Modulation of the EAP by an additional mutation in the selectivity filter and by mutations of Trp-1531 is shown. The stimulation protocol and depiction are the same as in B. A , residue

    Techniques Used: Binding Assay, Mutagenesis

    Mutations at Site 1575 Open an EAP for QX-222
    Figure Legend Snippet: Mutations at Site 1575 Open an EAP for QX-222

    Techniques Used:

    Effect of QX-222 on inactivation properties of channels carrying mutations at site 1531. A , in W1531A, 500 μ m QX-222 significantly shifted the steady-state inactivation curve to hyperpolarized potentials. V 1/2 was −74.6 ± 0.6 and
    Figure Legend Snippet: Effect of QX-222 on inactivation properties of channels carrying mutations at site 1531. A , in W1531A, 500 μ m QX-222 significantly shifted the steady-state inactivation curve to hyperpolarized potentials. V 1/2 was −74.6 ± 0.6 and

    Techniques Used:

    External block by QX-222 is favored by replacement of Ile-1575 with amino acids of small size or with hydrophilic properties. Sodium currents were evoked by depolarizing pulses at a frequency of 2 Hz (see “Experimental Procedures”). Connecting
    Figure Legend Snippet: External block by QX-222 is favored by replacement of Ile-1575 with amino acids of small size or with hydrophilic properties. Sodium currents were evoked by depolarizing pulses at a frequency of 2 Hz (see “Experimental Procedures”). Connecting

    Techniques Used: Blocking Assay

    Use-dependent block by external QX-222. A 2-Hz pulse train was applied for 30 s at a holding potential of −120 mV. Thereafter, external perfusion with QX-222 was started while cells were kept at the holding potential for 120 s. Then repetitive
    Figure Legend Snippet: Use-dependent block by external QX-222. A 2-Hz pulse train was applied for 30 s at a holding potential of −120 mV. Thereafter, external perfusion with QX-222 was started while cells were kept at the holding potential for 120 s. Then repetitive

    Techniques Used: Blocking Assay

    7) Product Images from "Exploring the Structure of the Voltage-gated Na+ Channel by an Engineered Drug Access Pathway to the Receptor Site for Local Anesthetics *"

    Article Title: Exploring the Structure of the Voltage-gated Na+ Channel by an Engineered Drug Access Pathway to the Receptor Site for Local Anesthetics *

    Journal: The Journal of Biological Chemistry

    doi: 10.1074/jbc.M113.541763

    Structure of the external access pathway. The proposed molecular arrangement of crucial amino acids involved in access and binding of QX-222 is shown. A and B ), respectively, based
    Figure Legend Snippet: Structure of the external access pathway. The proposed molecular arrangement of crucial amino acids involved in access and binding of QX-222 is shown. A and B ), respectively, based

    Techniques Used: Binding Assay

    Recovery from block by intracellular QX-222. A 5-s-long 10-Hz pulse train was applied for repetitive openings of the channels to bind QX-222 to the inner vestibule. After the last pulse in the train, the cell was repolarized to −140 mV for various
    Figure Legend Snippet: Recovery from block by intracellular QX-222. A 5-s-long 10-Hz pulse train was applied for repetitive openings of the channels to bind QX-222 to the inner vestibule. After the last pulse in the train, the cell was repolarized to −140 mV for various

    Techniques Used: Blocking Assay

    The binding site for external QX-222 is in the internal vestibule. Modulation of the EAP by an additional mutation in the selectivity filter and by mutations of Trp-1531 is shown. The stimulation protocol and depiction are the same as in B. A , residue
    Figure Legend Snippet: The binding site for external QX-222 is in the internal vestibule. Modulation of the EAP by an additional mutation in the selectivity filter and by mutations of Trp-1531 is shown. The stimulation protocol and depiction are the same as in B. A , residue

    Techniques Used: Binding Assay, Mutagenesis

    Mutations at Site 1575 Open an EAP for QX-222
    Figure Legend Snippet: Mutations at Site 1575 Open an EAP for QX-222

    Techniques Used:

    Effect of QX-222 on inactivation properties of channels carrying mutations at site 1531. A , in W1531A, 500 μ m QX-222 significantly shifted the steady-state inactivation curve to hyperpolarized potentials. V 1/2 was −74.6 ± 0.6 and
    Figure Legend Snippet: Effect of QX-222 on inactivation properties of channels carrying mutations at site 1531. A , in W1531A, 500 μ m QX-222 significantly shifted the steady-state inactivation curve to hyperpolarized potentials. V 1/2 was −74.6 ± 0.6 and

    Techniques Used:

    External block by QX-222 is favored by replacement of Ile-1575 with amino acids of small size or with hydrophilic properties. Sodium currents were evoked by depolarizing pulses at a frequency of 2 Hz (see “Experimental Procedures”). Connecting
    Figure Legend Snippet: External block by QX-222 is favored by replacement of Ile-1575 with amino acids of small size or with hydrophilic properties. Sodium currents were evoked by depolarizing pulses at a frequency of 2 Hz (see “Experimental Procedures”). Connecting

    Techniques Used: Blocking Assay

    Use-dependent block by external QX-222. A 2-Hz pulse train was applied for 30 s at a holding potential of −120 mV. Thereafter, external perfusion with QX-222 was started while cells were kept at the holding potential for 120 s. Then repetitive
    Figure Legend Snippet: Use-dependent block by external QX-222. A 2-Hz pulse train was applied for 30 s at a holding potential of −120 mV. Thereafter, external perfusion with QX-222 was started while cells were kept at the holding potential for 120 s. Then repetitive

    Techniques Used: Blocking Assay

    8) Product Images from "Exploring the Structure of the Voltage-gated Na+ Channel by an Engineered Drug Access Pathway to the Receptor Site for Local Anesthetics *"

    Article Title: Exploring the Structure of the Voltage-gated Na+ Channel by an Engineered Drug Access Pathway to the Receptor Site for Local Anesthetics *

    Journal: The Journal of Biological Chemistry

    doi: 10.1074/jbc.M113.541763

    Structure of the external access pathway. The proposed molecular arrangement of crucial amino acids involved in access and binding of QX-222 is shown. A and B ), respectively, based
    Figure Legend Snippet: Structure of the external access pathway. The proposed molecular arrangement of crucial amino acids involved in access and binding of QX-222 is shown. A and B ), respectively, based

    Techniques Used: Binding Assay

    Recovery from block by intracellular QX-222. A 5-s-long 10-Hz pulse train was applied for repetitive openings of the channels to bind QX-222 to the inner vestibule. After the last pulse in the train, the cell was repolarized to −140 mV for various
    Figure Legend Snippet: Recovery from block by intracellular QX-222. A 5-s-long 10-Hz pulse train was applied for repetitive openings of the channels to bind QX-222 to the inner vestibule. After the last pulse in the train, the cell was repolarized to −140 mV for various

    Techniques Used: Blocking Assay

    The binding site for external QX-222 is in the internal vestibule. Modulation of the EAP by an additional mutation in the selectivity filter and by mutations of Trp-1531 is shown. The stimulation protocol and depiction are the same as in B. A , residue
    Figure Legend Snippet: The binding site for external QX-222 is in the internal vestibule. Modulation of the EAP by an additional mutation in the selectivity filter and by mutations of Trp-1531 is shown. The stimulation protocol and depiction are the same as in B. A , residue

    Techniques Used: Binding Assay, Mutagenesis

    Mutations at Site 1575 Open an EAP for QX-222
    Figure Legend Snippet: Mutations at Site 1575 Open an EAP for QX-222

    Techniques Used:

    Effect of QX-222 on inactivation properties of channels carrying mutations at site 1531. A , in W1531A, 500 μ m QX-222 significantly shifted the steady-state inactivation curve to hyperpolarized potentials. V 1/2 was −74.6 ± 0.6 and
    Figure Legend Snippet: Effect of QX-222 on inactivation properties of channels carrying mutations at site 1531. A , in W1531A, 500 μ m QX-222 significantly shifted the steady-state inactivation curve to hyperpolarized potentials. V 1/2 was −74.6 ± 0.6 and

    Techniques Used:

    External block by QX-222 is favored by replacement of Ile-1575 with amino acids of small size or with hydrophilic properties. Sodium currents were evoked by depolarizing pulses at a frequency of 2 Hz (see “Experimental Procedures”). Connecting
    Figure Legend Snippet: External block by QX-222 is favored by replacement of Ile-1575 with amino acids of small size or with hydrophilic properties. Sodium currents were evoked by depolarizing pulses at a frequency of 2 Hz (see “Experimental Procedures”). Connecting

    Techniques Used: Blocking Assay

    Use-dependent block by external QX-222. A 2-Hz pulse train was applied for 30 s at a holding potential of −120 mV. Thereafter, external perfusion with QX-222 was started while cells were kept at the holding potential for 120 s. Then repetitive
    Figure Legend Snippet: Use-dependent block by external QX-222. A 2-Hz pulse train was applied for 30 s at a holding potential of −120 mV. Thereafter, external perfusion with QX-222 was started while cells were kept at the holding potential for 120 s. Then repetitive

    Techniques Used: Blocking Assay

    9) Product Images from "Exploring the Structure of the Voltage-gated Na+ Channel by an Engineered Drug Access Pathway to the Receptor Site for Local Anesthetics *"

    Article Title: Exploring the Structure of the Voltage-gated Na+ Channel by an Engineered Drug Access Pathway to the Receptor Site for Local Anesthetics *

    Journal: The Journal of Biological Chemistry

    doi: 10.1074/jbc.M113.541763

    Structure of the external access pathway. The proposed molecular arrangement of crucial amino acids involved in access and binding of QX-222 is shown. A and B ), respectively, based
    Figure Legend Snippet: Structure of the external access pathway. The proposed molecular arrangement of crucial amino acids involved in access and binding of QX-222 is shown. A and B ), respectively, based

    Techniques Used: Binding Assay

    Recovery from block by intracellular QX-222. A 5-s-long 10-Hz pulse train was applied for repetitive openings of the channels to bind QX-222 to the inner vestibule. After the last pulse in the train, the cell was repolarized to −140 mV for various
    Figure Legend Snippet: Recovery from block by intracellular QX-222. A 5-s-long 10-Hz pulse train was applied for repetitive openings of the channels to bind QX-222 to the inner vestibule. After the last pulse in the train, the cell was repolarized to −140 mV for various

    Techniques Used: Blocking Assay

    The binding site for external QX-222 is in the internal vestibule. Modulation of the EAP by an additional mutation in the selectivity filter and by mutations of Trp-1531 is shown. The stimulation protocol and depiction are the same as in B. A , residue
    Figure Legend Snippet: The binding site for external QX-222 is in the internal vestibule. Modulation of the EAP by an additional mutation in the selectivity filter and by mutations of Trp-1531 is shown. The stimulation protocol and depiction are the same as in B. A , residue

    Techniques Used: Binding Assay, Mutagenesis

    Mutations at Site 1575 Open an EAP for QX-222
    Figure Legend Snippet: Mutations at Site 1575 Open an EAP for QX-222

    Techniques Used:

    Effect of QX-222 on inactivation properties of channels carrying mutations at site 1531. A , in W1531A, 500 μ m QX-222 significantly shifted the steady-state inactivation curve to hyperpolarized potentials. V 1/2 was −74.6 ± 0.6 and
    Figure Legend Snippet: Effect of QX-222 on inactivation properties of channels carrying mutations at site 1531. A , in W1531A, 500 μ m QX-222 significantly shifted the steady-state inactivation curve to hyperpolarized potentials. V 1/2 was −74.6 ± 0.6 and

    Techniques Used:

    External block by QX-222 is favored by replacement of Ile-1575 with amino acids of small size or with hydrophilic properties. Sodium currents were evoked by depolarizing pulses at a frequency of 2 Hz (see “Experimental Procedures”). Connecting
    Figure Legend Snippet: External block by QX-222 is favored by replacement of Ile-1575 with amino acids of small size or with hydrophilic properties. Sodium currents were evoked by depolarizing pulses at a frequency of 2 Hz (see “Experimental Procedures”). Connecting

    Techniques Used: Blocking Assay

    Use-dependent block by external QX-222. A 2-Hz pulse train was applied for 30 s at a holding potential of −120 mV. Thereafter, external perfusion with QX-222 was started while cells were kept at the holding potential for 120 s. Then repetitive
    Figure Legend Snippet: Use-dependent block by external QX-222. A 2-Hz pulse train was applied for 30 s at a holding potential of −120 mV. Thereafter, external perfusion with QX-222 was started while cells were kept at the holding potential for 120 s. Then repetitive

    Techniques Used: Blocking Assay

    10) Product Images from "Exploring the Structure of the Voltage-gated Na+ Channel by an Engineered Drug Access Pathway to the Receptor Site for Local Anesthetics *"

    Article Title: Exploring the Structure of the Voltage-gated Na+ Channel by an Engineered Drug Access Pathway to the Receptor Site for Local Anesthetics *

    Journal: The Journal of Biological Chemistry

    doi: 10.1074/jbc.M113.541763

    Structure of the external access pathway. The proposed molecular arrangement of crucial amino acids involved in access and binding of QX-222 is shown. A and B ), respectively, based
    Figure Legend Snippet: Structure of the external access pathway. The proposed molecular arrangement of crucial amino acids involved in access and binding of QX-222 is shown. A and B ), respectively, based

    Techniques Used: Binding Assay

    Recovery from block by intracellular QX-222. A 5-s-long 10-Hz pulse train was applied for repetitive openings of the channels to bind QX-222 to the inner vestibule. After the last pulse in the train, the cell was repolarized to −140 mV for various
    Figure Legend Snippet: Recovery from block by intracellular QX-222. A 5-s-long 10-Hz pulse train was applied for repetitive openings of the channels to bind QX-222 to the inner vestibule. After the last pulse in the train, the cell was repolarized to −140 mV for various

    Techniques Used: Blocking Assay

    The binding site for external QX-222 is in the internal vestibule. Modulation of the EAP by an additional mutation in the selectivity filter and by mutations of Trp-1531 is shown. The stimulation protocol and depiction are the same as in B. A , residue
    Figure Legend Snippet: The binding site for external QX-222 is in the internal vestibule. Modulation of the EAP by an additional mutation in the selectivity filter and by mutations of Trp-1531 is shown. The stimulation protocol and depiction are the same as in B. A , residue

    Techniques Used: Binding Assay, Mutagenesis

    Mutations at Site 1575 Open an EAP for QX-222
    Figure Legend Snippet: Mutations at Site 1575 Open an EAP for QX-222

    Techniques Used:

    Effect of QX-222 on inactivation properties of channels carrying mutations at site 1531. A , in W1531A, 500 μ m QX-222 significantly shifted the steady-state inactivation curve to hyperpolarized potentials. V 1/2 was −74.6 ± 0.6 and
    Figure Legend Snippet: Effect of QX-222 on inactivation properties of channels carrying mutations at site 1531. A , in W1531A, 500 μ m QX-222 significantly shifted the steady-state inactivation curve to hyperpolarized potentials. V 1/2 was −74.6 ± 0.6 and

    Techniques Used:

    External block by QX-222 is favored by replacement of Ile-1575 with amino acids of small size or with hydrophilic properties. Sodium currents were evoked by depolarizing pulses at a frequency of 2 Hz (see “Experimental Procedures”). Connecting
    Figure Legend Snippet: External block by QX-222 is favored by replacement of Ile-1575 with amino acids of small size or with hydrophilic properties. Sodium currents were evoked by depolarizing pulses at a frequency of 2 Hz (see “Experimental Procedures”). Connecting

    Techniques Used: Blocking Assay

    Use-dependent block by external QX-222. A 2-Hz pulse train was applied for 30 s at a holding potential of −120 mV. Thereafter, external perfusion with QX-222 was started while cells were kept at the holding potential for 120 s. Then repetitive
    Figure Legend Snippet: Use-dependent block by external QX-222. A 2-Hz pulse train was applied for 30 s at a holding potential of −120 mV. Thereafter, external perfusion with QX-222 was started while cells were kept at the holding potential for 120 s. Then repetitive

    Techniques Used: Blocking Assay

    11) Product Images from "Exploring the Structure of the Voltage-gated Na+ Channel by an Engineered Drug Access Pathway to the Receptor Site for Local Anesthetics *"

    Article Title: Exploring the Structure of the Voltage-gated Na+ Channel by an Engineered Drug Access Pathway to the Receptor Site for Local Anesthetics *

    Journal: The Journal of Biological Chemistry

    doi: 10.1074/jbc.M113.541763

    Structure of the external access pathway. The proposed molecular arrangement of crucial amino acids involved in access and binding of QX-222 is shown. A and B ), respectively, based
    Figure Legend Snippet: Structure of the external access pathway. The proposed molecular arrangement of crucial amino acids involved in access and binding of QX-222 is shown. A and B ), respectively, based

    Techniques Used: Binding Assay

    Recovery from block by intracellular QX-222. A 5-s-long 10-Hz pulse train was applied for repetitive openings of the channels to bind QX-222 to the inner vestibule. After the last pulse in the train, the cell was repolarized to −140 mV for various
    Figure Legend Snippet: Recovery from block by intracellular QX-222. A 5-s-long 10-Hz pulse train was applied for repetitive openings of the channels to bind QX-222 to the inner vestibule. After the last pulse in the train, the cell was repolarized to −140 mV for various

    Techniques Used: Blocking Assay

    The binding site for external QX-222 is in the internal vestibule. Modulation of the EAP by an additional mutation in the selectivity filter and by mutations of Trp-1531 is shown. The stimulation protocol and depiction are the same as in B. A , residue
    Figure Legend Snippet: The binding site for external QX-222 is in the internal vestibule. Modulation of the EAP by an additional mutation in the selectivity filter and by mutations of Trp-1531 is shown. The stimulation protocol and depiction are the same as in B. A , residue

    Techniques Used: Binding Assay, Mutagenesis

    Mutations at Site 1575 Open an EAP for QX-222
    Figure Legend Snippet: Mutations at Site 1575 Open an EAP for QX-222

    Techniques Used:

    Effect of QX-222 on inactivation properties of channels carrying mutations at site 1531. A , in W1531A, 500 μ m QX-222 significantly shifted the steady-state inactivation curve to hyperpolarized potentials. V 1/2 was −74.6 ± 0.6 and
    Figure Legend Snippet: Effect of QX-222 on inactivation properties of channels carrying mutations at site 1531. A , in W1531A, 500 μ m QX-222 significantly shifted the steady-state inactivation curve to hyperpolarized potentials. V 1/2 was −74.6 ± 0.6 and

    Techniques Used:

    External block by QX-222 is favored by replacement of Ile-1575 with amino acids of small size or with hydrophilic properties. Sodium currents were evoked by depolarizing pulses at a frequency of 2 Hz (see “Experimental Procedures”). Connecting
    Figure Legend Snippet: External block by QX-222 is favored by replacement of Ile-1575 with amino acids of small size or with hydrophilic properties. Sodium currents were evoked by depolarizing pulses at a frequency of 2 Hz (see “Experimental Procedures”). Connecting

    Techniques Used: Blocking Assay

    Use-dependent block by external QX-222. A 2-Hz pulse train was applied for 30 s at a holding potential of −120 mV. Thereafter, external perfusion with QX-222 was started while cells were kept at the holding potential for 120 s. Then repetitive
    Figure Legend Snippet: Use-dependent block by external QX-222. A 2-Hz pulse train was applied for 30 s at a holding potential of −120 mV. Thereafter, external perfusion with QX-222 was started while cells were kept at the holding potential for 120 s. Then repetitive

    Techniques Used: Blocking Assay

    12) Product Images from "Exploring the Structure of the Voltage-gated Na+ Channel by an Engineered Drug Access Pathway to the Receptor Site for Local Anesthetics *"

    Article Title: Exploring the Structure of the Voltage-gated Na+ Channel by an Engineered Drug Access Pathway to the Receptor Site for Local Anesthetics *

    Journal: The Journal of Biological Chemistry

    doi: 10.1074/jbc.M113.541763

    Structure of the external access pathway. The proposed molecular arrangement of crucial amino acids involved in access and binding of QX-222 is shown. A and B ), respectively, based
    Figure Legend Snippet: Structure of the external access pathway. The proposed molecular arrangement of crucial amino acids involved in access and binding of QX-222 is shown. A and B ), respectively, based

    Techniques Used: Binding Assay

    Recovery from block by intracellular QX-222. A 5-s-long 10-Hz pulse train was applied for repetitive openings of the channels to bind QX-222 to the inner vestibule. After the last pulse in the train, the cell was repolarized to −140 mV for various
    Figure Legend Snippet: Recovery from block by intracellular QX-222. A 5-s-long 10-Hz pulse train was applied for repetitive openings of the channels to bind QX-222 to the inner vestibule. After the last pulse in the train, the cell was repolarized to −140 mV for various

    Techniques Used: Blocking Assay

    The binding site for external QX-222 is in the internal vestibule. Modulation of the EAP by an additional mutation in the selectivity filter and by mutations of Trp-1531 is shown. The stimulation protocol and depiction are the same as in B. A , residue
    Figure Legend Snippet: The binding site for external QX-222 is in the internal vestibule. Modulation of the EAP by an additional mutation in the selectivity filter and by mutations of Trp-1531 is shown. The stimulation protocol and depiction are the same as in B. A , residue

    Techniques Used: Binding Assay, Mutagenesis

    Mutations at Site 1575 Open an EAP for QX-222
    Figure Legend Snippet: Mutations at Site 1575 Open an EAP for QX-222

    Techniques Used:

    Effect of QX-222 on inactivation properties of channels carrying mutations at site 1531. A , in W1531A, 500 μ m QX-222 significantly shifted the steady-state inactivation curve to hyperpolarized potentials. V 1/2 was −74.6 ± 0.6 and
    Figure Legend Snippet: Effect of QX-222 on inactivation properties of channels carrying mutations at site 1531. A , in W1531A, 500 μ m QX-222 significantly shifted the steady-state inactivation curve to hyperpolarized potentials. V 1/2 was −74.6 ± 0.6 and

    Techniques Used:

    External block by QX-222 is favored by replacement of Ile-1575 with amino acids of small size or with hydrophilic properties. Sodium currents were evoked by depolarizing pulses at a frequency of 2 Hz (see “Experimental Procedures”). Connecting
    Figure Legend Snippet: External block by QX-222 is favored by replacement of Ile-1575 with amino acids of small size or with hydrophilic properties. Sodium currents were evoked by depolarizing pulses at a frequency of 2 Hz (see “Experimental Procedures”). Connecting

    Techniques Used: Blocking Assay

    Use-dependent block by external QX-222. A 2-Hz pulse train was applied for 30 s at a holding potential of −120 mV. Thereafter, external perfusion with QX-222 was started while cells were kept at the holding potential for 120 s. Then repetitive
    Figure Legend Snippet: Use-dependent block by external QX-222. A 2-Hz pulse train was applied for 30 s at a holding potential of −120 mV. Thereafter, external perfusion with QX-222 was started while cells were kept at the holding potential for 120 s. Then repetitive

    Techniques Used: Blocking Assay

    13) Product Images from "Exploring the Structure of the Voltage-gated Na+ Channel by an Engineered Drug Access Pathway to the Receptor Site for Local Anesthetics *"

    Article Title: Exploring the Structure of the Voltage-gated Na+ Channel by an Engineered Drug Access Pathway to the Receptor Site for Local Anesthetics *

    Journal: The Journal of Biological Chemistry

    doi: 10.1074/jbc.M113.541763

    Structure of the external access pathway. The proposed molecular arrangement of crucial amino acids involved in access and binding of QX-222 is shown. A and B ), respectively, based
    Figure Legend Snippet: Structure of the external access pathway. The proposed molecular arrangement of crucial amino acids involved in access and binding of QX-222 is shown. A and B ), respectively, based

    Techniques Used: Binding Assay

    Recovery from block by intracellular QX-222. A 5-s-long 10-Hz pulse train was applied for repetitive openings of the channels to bind QX-222 to the inner vestibule. After the last pulse in the train, the cell was repolarized to −140 mV for various
    Figure Legend Snippet: Recovery from block by intracellular QX-222. A 5-s-long 10-Hz pulse train was applied for repetitive openings of the channels to bind QX-222 to the inner vestibule. After the last pulse in the train, the cell was repolarized to −140 mV for various

    Techniques Used: Blocking Assay

    The binding site for external QX-222 is in the internal vestibule. Modulation of the EAP by an additional mutation in the selectivity filter and by mutations of Trp-1531 is shown. The stimulation protocol and depiction are the same as in B. A , residue
    Figure Legend Snippet: The binding site for external QX-222 is in the internal vestibule. Modulation of the EAP by an additional mutation in the selectivity filter and by mutations of Trp-1531 is shown. The stimulation protocol and depiction are the same as in B. A , residue

    Techniques Used: Binding Assay, Mutagenesis

    Mutations at Site 1575 Open an EAP for QX-222
    Figure Legend Snippet: Mutations at Site 1575 Open an EAP for QX-222

    Techniques Used:

    Effect of QX-222 on inactivation properties of channels carrying mutations at site 1531. A , in W1531A, 500 μ m QX-222 significantly shifted the steady-state inactivation curve to hyperpolarized potentials. V 1/2 was −74.6 ± 0.6 and
    Figure Legend Snippet: Effect of QX-222 on inactivation properties of channels carrying mutations at site 1531. A , in W1531A, 500 μ m QX-222 significantly shifted the steady-state inactivation curve to hyperpolarized potentials. V 1/2 was −74.6 ± 0.6 and

    Techniques Used:

    External block by QX-222 is favored by replacement of Ile-1575 with amino acids of small size or with hydrophilic properties. Sodium currents were evoked by depolarizing pulses at a frequency of 2 Hz (see “Experimental Procedures”). Connecting
    Figure Legend Snippet: External block by QX-222 is favored by replacement of Ile-1575 with amino acids of small size or with hydrophilic properties. Sodium currents were evoked by depolarizing pulses at a frequency of 2 Hz (see “Experimental Procedures”). Connecting

    Techniques Used: Blocking Assay

    Use-dependent block by external QX-222. A 2-Hz pulse train was applied for 30 s at a holding potential of −120 mV. Thereafter, external perfusion with QX-222 was started while cells were kept at the holding potential for 120 s. Then repetitive
    Figure Legend Snippet: Use-dependent block by external QX-222. A 2-Hz pulse train was applied for 30 s at a holding potential of −120 mV. Thereafter, external perfusion with QX-222 was started while cells were kept at the holding potential for 120 s. Then repetitive

    Techniques Used: Blocking Assay

    14) Product Images from "Exploring the Structure of the Voltage-gated Na+ Channel by an Engineered Drug Access Pathway to the Receptor Site for Local Anesthetics *"

    Article Title: Exploring the Structure of the Voltage-gated Na+ Channel by an Engineered Drug Access Pathway to the Receptor Site for Local Anesthetics *

    Journal: The Journal of Biological Chemistry

    doi: 10.1074/jbc.M113.541763

    Structure of the external access pathway. The proposed molecular arrangement of crucial amino acids involved in access and binding of QX-222 is shown. A and B ), respectively, based
    Figure Legend Snippet: Structure of the external access pathway. The proposed molecular arrangement of crucial amino acids involved in access and binding of QX-222 is shown. A and B ), respectively, based

    Techniques Used: Binding Assay

    Recovery from block by intracellular QX-222. A 5-s-long 10-Hz pulse train was applied for repetitive openings of the channels to bind QX-222 to the inner vestibule. After the last pulse in the train, the cell was repolarized to −140 mV for various
    Figure Legend Snippet: Recovery from block by intracellular QX-222. A 5-s-long 10-Hz pulse train was applied for repetitive openings of the channels to bind QX-222 to the inner vestibule. After the last pulse in the train, the cell was repolarized to −140 mV for various

    Techniques Used: Blocking Assay

    The binding site for external QX-222 is in the internal vestibule. Modulation of the EAP by an additional mutation in the selectivity filter and by mutations of Trp-1531 is shown. The stimulation protocol and depiction are the same as in B. A , residue
    Figure Legend Snippet: The binding site for external QX-222 is in the internal vestibule. Modulation of the EAP by an additional mutation in the selectivity filter and by mutations of Trp-1531 is shown. The stimulation protocol and depiction are the same as in B. A , residue

    Techniques Used: Binding Assay, Mutagenesis

    Mutations at Site 1575 Open an EAP for QX-222
    Figure Legend Snippet: Mutations at Site 1575 Open an EAP for QX-222

    Techniques Used:

    Effect of QX-222 on inactivation properties of channels carrying mutations at site 1531. A , in W1531A, 500 μ m QX-222 significantly shifted the steady-state inactivation curve to hyperpolarized potentials. V 1/2 was −74.6 ± 0.6 and
    Figure Legend Snippet: Effect of QX-222 on inactivation properties of channels carrying mutations at site 1531. A , in W1531A, 500 μ m QX-222 significantly shifted the steady-state inactivation curve to hyperpolarized potentials. V 1/2 was −74.6 ± 0.6 and

    Techniques Used:

    External block by QX-222 is favored by replacement of Ile-1575 with amino acids of small size or with hydrophilic properties. Sodium currents were evoked by depolarizing pulses at a frequency of 2 Hz (see “Experimental Procedures”). Connecting
    Figure Legend Snippet: External block by QX-222 is favored by replacement of Ile-1575 with amino acids of small size or with hydrophilic properties. Sodium currents were evoked by depolarizing pulses at a frequency of 2 Hz (see “Experimental Procedures”). Connecting

    Techniques Used: Blocking Assay

    Use-dependent block by external QX-222. A 2-Hz pulse train was applied for 30 s at a holding potential of −120 mV. Thereafter, external perfusion with QX-222 was started while cells were kept at the holding potential for 120 s. Then repetitive
    Figure Legend Snippet: Use-dependent block by external QX-222. A 2-Hz pulse train was applied for 30 s at a holding potential of −120 mV. Thereafter, external perfusion with QX-222 was started while cells were kept at the holding potential for 120 s. Then repetitive

    Techniques Used: Blocking Assay

    15) Product Images from "Exploring the Structure of the Voltage-gated Na+ Channel by an Engineered Drug Access Pathway to the Receptor Site for Local Anesthetics *"

    Article Title: Exploring the Structure of the Voltage-gated Na+ Channel by an Engineered Drug Access Pathway to the Receptor Site for Local Anesthetics *

    Journal: The Journal of Biological Chemistry

    doi: 10.1074/jbc.M113.541763

    Structure of the external access pathway. The proposed molecular arrangement of crucial amino acids involved in access and binding of QX-222 is shown. A and B ), respectively, based
    Figure Legend Snippet: Structure of the external access pathway. The proposed molecular arrangement of crucial amino acids involved in access and binding of QX-222 is shown. A and B ), respectively, based

    Techniques Used: Binding Assay

    Recovery from block by intracellular QX-222. A 5-s-long 10-Hz pulse train was applied for repetitive openings of the channels to bind QX-222 to the inner vestibule. After the last pulse in the train, the cell was repolarized to −140 mV for various
    Figure Legend Snippet: Recovery from block by intracellular QX-222. A 5-s-long 10-Hz pulse train was applied for repetitive openings of the channels to bind QX-222 to the inner vestibule. After the last pulse in the train, the cell was repolarized to −140 mV for various

    Techniques Used: Blocking Assay

    The binding site for external QX-222 is in the internal vestibule. Modulation of the EAP by an additional mutation in the selectivity filter and by mutations of Trp-1531 is shown. The stimulation protocol and depiction are the same as in B. A , residue
    Figure Legend Snippet: The binding site for external QX-222 is in the internal vestibule. Modulation of the EAP by an additional mutation in the selectivity filter and by mutations of Trp-1531 is shown. The stimulation protocol and depiction are the same as in B. A , residue

    Techniques Used: Binding Assay, Mutagenesis

    Mutations at Site 1575 Open an EAP for QX-222
    Figure Legend Snippet: Mutations at Site 1575 Open an EAP for QX-222

    Techniques Used:

    Effect of QX-222 on inactivation properties of channels carrying mutations at site 1531. A , in W1531A, 500 μ m QX-222 significantly shifted the steady-state inactivation curve to hyperpolarized potentials. V 1/2 was −74.6 ± 0.6 and
    Figure Legend Snippet: Effect of QX-222 on inactivation properties of channels carrying mutations at site 1531. A , in W1531A, 500 μ m QX-222 significantly shifted the steady-state inactivation curve to hyperpolarized potentials. V 1/2 was −74.6 ± 0.6 and

    Techniques Used:

    External block by QX-222 is favored by replacement of Ile-1575 with amino acids of small size or with hydrophilic properties. Sodium currents were evoked by depolarizing pulses at a frequency of 2 Hz (see “Experimental Procedures”). Connecting
    Figure Legend Snippet: External block by QX-222 is favored by replacement of Ile-1575 with amino acids of small size or with hydrophilic properties. Sodium currents were evoked by depolarizing pulses at a frequency of 2 Hz (see “Experimental Procedures”). Connecting

    Techniques Used: Blocking Assay

    Use-dependent block by external QX-222. A 2-Hz pulse train was applied for 30 s at a holding potential of −120 mV. Thereafter, external perfusion with QX-222 was started while cells were kept at the holding potential for 120 s. Then repetitive
    Figure Legend Snippet: Use-dependent block by external QX-222. A 2-Hz pulse train was applied for 30 s at a holding potential of −120 mV. Thereafter, external perfusion with QX-222 was started while cells were kept at the holding potential for 120 s. Then repetitive

    Techniques Used: Blocking Assay

    16) Product Images from "Exploring the Structure of the Voltage-gated Na+ Channel by an Engineered Drug Access Pathway to the Receptor Site for Local Anesthetics *"

    Article Title: Exploring the Structure of the Voltage-gated Na+ Channel by an Engineered Drug Access Pathway to the Receptor Site for Local Anesthetics *

    Journal: The Journal of Biological Chemistry

    doi: 10.1074/jbc.M113.541763

    Structure of the external access pathway. The proposed molecular arrangement of crucial amino acids involved in access and binding of QX-222 is shown. A and B ), respectively, based
    Figure Legend Snippet: Structure of the external access pathway. The proposed molecular arrangement of crucial amino acids involved in access and binding of QX-222 is shown. A and B ), respectively, based

    Techniques Used: Binding Assay

    Recovery from block by intracellular QX-222. A 5-s-long 10-Hz pulse train was applied for repetitive openings of the channels to bind QX-222 to the inner vestibule. After the last pulse in the train, the cell was repolarized to −140 mV for various
    Figure Legend Snippet: Recovery from block by intracellular QX-222. A 5-s-long 10-Hz pulse train was applied for repetitive openings of the channels to bind QX-222 to the inner vestibule. After the last pulse in the train, the cell was repolarized to −140 mV for various

    Techniques Used: Blocking Assay

    The binding site for external QX-222 is in the internal vestibule. Modulation of the EAP by an additional mutation in the selectivity filter and by mutations of Trp-1531 is shown. The stimulation protocol and depiction are the same as in B. A , residue
    Figure Legend Snippet: The binding site for external QX-222 is in the internal vestibule. Modulation of the EAP by an additional mutation in the selectivity filter and by mutations of Trp-1531 is shown. The stimulation protocol and depiction are the same as in B. A , residue

    Techniques Used: Binding Assay, Mutagenesis

    Mutations at Site 1575 Open an EAP for QX-222
    Figure Legend Snippet: Mutations at Site 1575 Open an EAP for QX-222

    Techniques Used:

    Effect of QX-222 on inactivation properties of channels carrying mutations at site 1531. A , in W1531A, 500 μ m QX-222 significantly shifted the steady-state inactivation curve to hyperpolarized potentials. V 1/2 was −74.6 ± 0.6 and
    Figure Legend Snippet: Effect of QX-222 on inactivation properties of channels carrying mutations at site 1531. A , in W1531A, 500 μ m QX-222 significantly shifted the steady-state inactivation curve to hyperpolarized potentials. V 1/2 was −74.6 ± 0.6 and

    Techniques Used:

    External block by QX-222 is favored by replacement of Ile-1575 with amino acids of small size or with hydrophilic properties. Sodium currents were evoked by depolarizing pulses at a frequency of 2 Hz (see “Experimental Procedures”). Connecting
    Figure Legend Snippet: External block by QX-222 is favored by replacement of Ile-1575 with amino acids of small size or with hydrophilic properties. Sodium currents were evoked by depolarizing pulses at a frequency of 2 Hz (see “Experimental Procedures”). Connecting

    Techniques Used: Blocking Assay

    Use-dependent block by external QX-222. A 2-Hz pulse train was applied for 30 s at a holding potential of −120 mV. Thereafter, external perfusion with QX-222 was started while cells were kept at the holding potential for 120 s. Then repetitive
    Figure Legend Snippet: Use-dependent block by external QX-222. A 2-Hz pulse train was applied for 30 s at a holding potential of −120 mV. Thereafter, external perfusion with QX-222 was started while cells were kept at the holding potential for 120 s. Then repetitive

    Techniques Used: Blocking Assay

    17) Product Images from "Exploring the Structure of the Voltage-gated Na+ Channel by an Engineered Drug Access Pathway to the Receptor Site for Local Anesthetics *"

    Article Title: Exploring the Structure of the Voltage-gated Na+ Channel by an Engineered Drug Access Pathway to the Receptor Site for Local Anesthetics *

    Journal: The Journal of Biological Chemistry

    doi: 10.1074/jbc.M113.541763

    Structure of the external access pathway. The proposed molecular arrangement of crucial amino acids involved in access and binding of QX-222 is shown. A and B ), respectively, based
    Figure Legend Snippet: Structure of the external access pathway. The proposed molecular arrangement of crucial amino acids involved in access and binding of QX-222 is shown. A and B ), respectively, based

    Techniques Used: Binding Assay

    Recovery from block by intracellular QX-222. A 5-s-long 10-Hz pulse train was applied for repetitive openings of the channels to bind QX-222 to the inner vestibule. After the last pulse in the train, the cell was repolarized to −140 mV for various
    Figure Legend Snippet: Recovery from block by intracellular QX-222. A 5-s-long 10-Hz pulse train was applied for repetitive openings of the channels to bind QX-222 to the inner vestibule. After the last pulse in the train, the cell was repolarized to −140 mV for various

    Techniques Used: Blocking Assay

    The binding site for external QX-222 is in the internal vestibule. Modulation of the EAP by an additional mutation in the selectivity filter and by mutations of Trp-1531 is shown. The stimulation protocol and depiction are the same as in B. A , residue
    Figure Legend Snippet: The binding site for external QX-222 is in the internal vestibule. Modulation of the EAP by an additional mutation in the selectivity filter and by mutations of Trp-1531 is shown. The stimulation protocol and depiction are the same as in B. A , residue

    Techniques Used: Binding Assay, Mutagenesis

    Mutations at Site 1575 Open an EAP for QX-222
    Figure Legend Snippet: Mutations at Site 1575 Open an EAP for QX-222

    Techniques Used:

    Effect of QX-222 on inactivation properties of channels carrying mutations at site 1531. A , in W1531A, 500 μ m QX-222 significantly shifted the steady-state inactivation curve to hyperpolarized potentials. V 1/2 was −74.6 ± 0.6 and
    Figure Legend Snippet: Effect of QX-222 on inactivation properties of channels carrying mutations at site 1531. A , in W1531A, 500 μ m QX-222 significantly shifted the steady-state inactivation curve to hyperpolarized potentials. V 1/2 was −74.6 ± 0.6 and

    Techniques Used:

    External block by QX-222 is favored by replacement of Ile-1575 with amino acids of small size or with hydrophilic properties. Sodium currents were evoked by depolarizing pulses at a frequency of 2 Hz (see “Experimental Procedures”). Connecting
    Figure Legend Snippet: External block by QX-222 is favored by replacement of Ile-1575 with amino acids of small size or with hydrophilic properties. Sodium currents were evoked by depolarizing pulses at a frequency of 2 Hz (see “Experimental Procedures”). Connecting

    Techniques Used: Blocking Assay

    Use-dependent block by external QX-222. A 2-Hz pulse train was applied for 30 s at a holding potential of −120 mV. Thereafter, external perfusion with QX-222 was started while cells were kept at the holding potential for 120 s. Then repetitive
    Figure Legend Snippet: Use-dependent block by external QX-222. A 2-Hz pulse train was applied for 30 s at a holding potential of −120 mV. Thereafter, external perfusion with QX-222 was started while cells were kept at the holding potential for 120 s. Then repetitive

    Techniques Used: Blocking Assay

    18) Product Images from "Exploring the Structure of the Voltage-gated Na+ Channel by an Engineered Drug Access Pathway to the Receptor Site for Local Anesthetics *"

    Article Title: Exploring the Structure of the Voltage-gated Na+ Channel by an Engineered Drug Access Pathway to the Receptor Site for Local Anesthetics *

    Journal: The Journal of Biological Chemistry

    doi: 10.1074/jbc.M113.541763

    Structure of the external access pathway. The proposed molecular arrangement of crucial amino acids involved in access and binding of QX-222 is shown. A and B ), respectively, based
    Figure Legend Snippet: Structure of the external access pathway. The proposed molecular arrangement of crucial amino acids involved in access and binding of QX-222 is shown. A and B ), respectively, based

    Techniques Used: Binding Assay

    Recovery from block by intracellular QX-222. A 5-s-long 10-Hz pulse train was applied for repetitive openings of the channels to bind QX-222 to the inner vestibule. After the last pulse in the train, the cell was repolarized to −140 mV for various
    Figure Legend Snippet: Recovery from block by intracellular QX-222. A 5-s-long 10-Hz pulse train was applied for repetitive openings of the channels to bind QX-222 to the inner vestibule. After the last pulse in the train, the cell was repolarized to −140 mV for various

    Techniques Used: Blocking Assay

    The binding site for external QX-222 is in the internal vestibule. Modulation of the EAP by an additional mutation in the selectivity filter and by mutations of Trp-1531 is shown. The stimulation protocol and depiction are the same as in B. A , residue
    Figure Legend Snippet: The binding site for external QX-222 is in the internal vestibule. Modulation of the EAP by an additional mutation in the selectivity filter and by mutations of Trp-1531 is shown. The stimulation protocol and depiction are the same as in B. A , residue

    Techniques Used: Binding Assay, Mutagenesis

    Mutations at Site 1575 Open an EAP for QX-222
    Figure Legend Snippet: Mutations at Site 1575 Open an EAP for QX-222

    Techniques Used:

    Effect of QX-222 on inactivation properties of channels carrying mutations at site 1531. A , in W1531A, 500 μ m QX-222 significantly shifted the steady-state inactivation curve to hyperpolarized potentials. V 1/2 was −74.6 ± 0.6 and
    Figure Legend Snippet: Effect of QX-222 on inactivation properties of channels carrying mutations at site 1531. A , in W1531A, 500 μ m QX-222 significantly shifted the steady-state inactivation curve to hyperpolarized potentials. V 1/2 was −74.6 ± 0.6 and

    Techniques Used:

    External block by QX-222 is favored by replacement of Ile-1575 with amino acids of small size or with hydrophilic properties. Sodium currents were evoked by depolarizing pulses at a frequency of 2 Hz (see “Experimental Procedures”). Connecting
    Figure Legend Snippet: External block by QX-222 is favored by replacement of Ile-1575 with amino acids of small size or with hydrophilic properties. Sodium currents were evoked by depolarizing pulses at a frequency of 2 Hz (see “Experimental Procedures”). Connecting

    Techniques Used: Blocking Assay

    Use-dependent block by external QX-222. A 2-Hz pulse train was applied for 30 s at a holding potential of −120 mV. Thereafter, external perfusion with QX-222 was started while cells were kept at the holding potential for 120 s. Then repetitive
    Figure Legend Snippet: Use-dependent block by external QX-222. A 2-Hz pulse train was applied for 30 s at a holding potential of −120 mV. Thereafter, external perfusion with QX-222 was started while cells were kept at the holding potential for 120 s. Then repetitive

    Techniques Used: Blocking Assay

    19) Product Images from "Exploring the Structure of the Voltage-gated Na+ Channel by an Engineered Drug Access Pathway to the Receptor Site for Local Anesthetics *"

    Article Title: Exploring the Structure of the Voltage-gated Na+ Channel by an Engineered Drug Access Pathway to the Receptor Site for Local Anesthetics *

    Journal: The Journal of Biological Chemistry

    doi: 10.1074/jbc.M113.541763

    Structure of the external access pathway. The proposed molecular arrangement of crucial amino acids involved in access and binding of QX-222 is shown. A and B ), respectively, based
    Figure Legend Snippet: Structure of the external access pathway. The proposed molecular arrangement of crucial amino acids involved in access and binding of QX-222 is shown. A and B ), respectively, based

    Techniques Used: Binding Assay

    Recovery from block by intracellular QX-222. A 5-s-long 10-Hz pulse train was applied for repetitive openings of the channels to bind QX-222 to the inner vestibule. After the last pulse in the train, the cell was repolarized to −140 mV for various
    Figure Legend Snippet: Recovery from block by intracellular QX-222. A 5-s-long 10-Hz pulse train was applied for repetitive openings of the channels to bind QX-222 to the inner vestibule. After the last pulse in the train, the cell was repolarized to −140 mV for various

    Techniques Used: Blocking Assay

    The binding site for external QX-222 is in the internal vestibule. Modulation of the EAP by an additional mutation in the selectivity filter and by mutations of Trp-1531 is shown. The stimulation protocol and depiction are the same as in B. A , residue
    Figure Legend Snippet: The binding site for external QX-222 is in the internal vestibule. Modulation of the EAP by an additional mutation in the selectivity filter and by mutations of Trp-1531 is shown. The stimulation protocol and depiction are the same as in B. A , residue

    Techniques Used: Binding Assay, Mutagenesis

    Mutations at Site 1575 Open an EAP for QX-222
    Figure Legend Snippet: Mutations at Site 1575 Open an EAP for QX-222

    Techniques Used:

    Effect of QX-222 on inactivation properties of channels carrying mutations at site 1531. A , in W1531A, 500 μ m QX-222 significantly shifted the steady-state inactivation curve to hyperpolarized potentials. V 1/2 was −74.6 ± 0.6 and
    Figure Legend Snippet: Effect of QX-222 on inactivation properties of channels carrying mutations at site 1531. A , in W1531A, 500 μ m QX-222 significantly shifted the steady-state inactivation curve to hyperpolarized potentials. V 1/2 was −74.6 ± 0.6 and

    Techniques Used:

    External block by QX-222 is favored by replacement of Ile-1575 with amino acids of small size or with hydrophilic properties. Sodium currents were evoked by depolarizing pulses at a frequency of 2 Hz (see “Experimental Procedures”). Connecting
    Figure Legend Snippet: External block by QX-222 is favored by replacement of Ile-1575 with amino acids of small size or with hydrophilic properties. Sodium currents were evoked by depolarizing pulses at a frequency of 2 Hz (see “Experimental Procedures”). Connecting

    Techniques Used: Blocking Assay

    Use-dependent block by external QX-222. A 2-Hz pulse train was applied for 30 s at a holding potential of −120 mV. Thereafter, external perfusion with QX-222 was started while cells were kept at the holding potential for 120 s. Then repetitive
    Figure Legend Snippet: Use-dependent block by external QX-222. A 2-Hz pulse train was applied for 30 s at a holding potential of −120 mV. Thereafter, external perfusion with QX-222 was started while cells were kept at the holding potential for 120 s. Then repetitive

    Techniques Used: Blocking Assay

    20) Product Images from "Exploring the Structure of the Voltage-gated Na+ Channel by an Engineered Drug Access Pathway to the Receptor Site for Local Anesthetics *"

    Article Title: Exploring the Structure of the Voltage-gated Na+ Channel by an Engineered Drug Access Pathway to the Receptor Site for Local Anesthetics *

    Journal: The Journal of Biological Chemistry

    doi: 10.1074/jbc.M113.541763

    Structure of the external access pathway. The proposed molecular arrangement of crucial amino acids involved in access and binding of QX-222 is shown. A and B ), respectively, based
    Figure Legend Snippet: Structure of the external access pathway. The proposed molecular arrangement of crucial amino acids involved in access and binding of QX-222 is shown. A and B ), respectively, based

    Techniques Used: Binding Assay

    Recovery from block by intracellular QX-222. A 5-s-long 10-Hz pulse train was applied for repetitive openings of the channels to bind QX-222 to the inner vestibule. After the last pulse in the train, the cell was repolarized to −140 mV for various
    Figure Legend Snippet: Recovery from block by intracellular QX-222. A 5-s-long 10-Hz pulse train was applied for repetitive openings of the channels to bind QX-222 to the inner vestibule. After the last pulse in the train, the cell was repolarized to −140 mV for various

    Techniques Used: Blocking Assay

    The binding site for external QX-222 is in the internal vestibule. Modulation of the EAP by an additional mutation in the selectivity filter and by mutations of Trp-1531 is shown. The stimulation protocol and depiction are the same as in B. A , residue
    Figure Legend Snippet: The binding site for external QX-222 is in the internal vestibule. Modulation of the EAP by an additional mutation in the selectivity filter and by mutations of Trp-1531 is shown. The stimulation protocol and depiction are the same as in B. A , residue

    Techniques Used: Binding Assay, Mutagenesis

    Mutations at Site 1575 Open an EAP for QX-222
    Figure Legend Snippet: Mutations at Site 1575 Open an EAP for QX-222

    Techniques Used:

    Effect of QX-222 on inactivation properties of channels carrying mutations at site 1531. A , in W1531A, 500 μ m QX-222 significantly shifted the steady-state inactivation curve to hyperpolarized potentials. V 1/2 was −74.6 ± 0.6 and
    Figure Legend Snippet: Effect of QX-222 on inactivation properties of channels carrying mutations at site 1531. A , in W1531A, 500 μ m QX-222 significantly shifted the steady-state inactivation curve to hyperpolarized potentials. V 1/2 was −74.6 ± 0.6 and

    Techniques Used:

    External block by QX-222 is favored by replacement of Ile-1575 with amino acids of small size or with hydrophilic properties. Sodium currents were evoked by depolarizing pulses at a frequency of 2 Hz (see “Experimental Procedures”). Connecting
    Figure Legend Snippet: External block by QX-222 is favored by replacement of Ile-1575 with amino acids of small size or with hydrophilic properties. Sodium currents were evoked by depolarizing pulses at a frequency of 2 Hz (see “Experimental Procedures”). Connecting

    Techniques Used: Blocking Assay

    Use-dependent block by external QX-222. A 2-Hz pulse train was applied for 30 s at a holding potential of −120 mV. Thereafter, external perfusion with QX-222 was started while cells were kept at the holding potential for 120 s. Then repetitive
    Figure Legend Snippet: Use-dependent block by external QX-222. A 2-Hz pulse train was applied for 30 s at a holding potential of −120 mV. Thereafter, external perfusion with QX-222 was started while cells were kept at the holding potential for 120 s. Then repetitive

    Techniques Used: Blocking Assay

    21) Product Images from "Exploring the Structure of the Voltage-gated Na+ Channel by an Engineered Drug Access Pathway to the Receptor Site for Local Anesthetics *"

    Article Title: Exploring the Structure of the Voltage-gated Na+ Channel by an Engineered Drug Access Pathway to the Receptor Site for Local Anesthetics *

    Journal: The Journal of Biological Chemistry

    doi: 10.1074/jbc.M113.541763

    Structure of the external access pathway. The proposed molecular arrangement of crucial amino acids involved in access and binding of QX-222 is shown. A and B ), respectively, based
    Figure Legend Snippet: Structure of the external access pathway. The proposed molecular arrangement of crucial amino acids involved in access and binding of QX-222 is shown. A and B ), respectively, based

    Techniques Used: Binding Assay

    Recovery from block by intracellular QX-222. A 5-s-long 10-Hz pulse train was applied for repetitive openings of the channels to bind QX-222 to the inner vestibule. After the last pulse in the train, the cell was repolarized to −140 mV for various
    Figure Legend Snippet: Recovery from block by intracellular QX-222. A 5-s-long 10-Hz pulse train was applied for repetitive openings of the channels to bind QX-222 to the inner vestibule. After the last pulse in the train, the cell was repolarized to −140 mV for various

    Techniques Used: Blocking Assay

    The binding site for external QX-222 is in the internal vestibule. Modulation of the EAP by an additional mutation in the selectivity filter and by mutations of Trp-1531 is shown. The stimulation protocol and depiction are the same as in B. A , residue
    Figure Legend Snippet: The binding site for external QX-222 is in the internal vestibule. Modulation of the EAP by an additional mutation in the selectivity filter and by mutations of Trp-1531 is shown. The stimulation protocol and depiction are the same as in B. A , residue

    Techniques Used: Binding Assay, Mutagenesis

    Mutations at Site 1575 Open an EAP for QX-222
    Figure Legend Snippet: Mutations at Site 1575 Open an EAP for QX-222

    Techniques Used:

    Effect of QX-222 on inactivation properties of channels carrying mutations at site 1531. A , in W1531A, 500 μ m QX-222 significantly shifted the steady-state inactivation curve to hyperpolarized potentials. V 1/2 was −74.6 ± 0.6 and
    Figure Legend Snippet: Effect of QX-222 on inactivation properties of channels carrying mutations at site 1531. A , in W1531A, 500 μ m QX-222 significantly shifted the steady-state inactivation curve to hyperpolarized potentials. V 1/2 was −74.6 ± 0.6 and

    Techniques Used:

    External block by QX-222 is favored by replacement of Ile-1575 with amino acids of small size or with hydrophilic properties. Sodium currents were evoked by depolarizing pulses at a frequency of 2 Hz (see “Experimental Procedures”). Connecting
    Figure Legend Snippet: External block by QX-222 is favored by replacement of Ile-1575 with amino acids of small size or with hydrophilic properties. Sodium currents were evoked by depolarizing pulses at a frequency of 2 Hz (see “Experimental Procedures”). Connecting

    Techniques Used: Blocking Assay

    Use-dependent block by external QX-222. A 2-Hz pulse train was applied for 30 s at a holding potential of −120 mV. Thereafter, external perfusion with QX-222 was started while cells were kept at the holding potential for 120 s. Then repetitive
    Figure Legend Snippet: Use-dependent block by external QX-222. A 2-Hz pulse train was applied for 30 s at a holding potential of −120 mV. Thereafter, external perfusion with QX-222 was started while cells were kept at the holding potential for 120 s. Then repetitive

    Techniques Used: Blocking Assay

    22) Product Images from "Exploring the Structure of the Voltage-gated Na+ Channel by an Engineered Drug Access Pathway to the Receptor Site for Local Anesthetics *"

    Article Title: Exploring the Structure of the Voltage-gated Na+ Channel by an Engineered Drug Access Pathway to the Receptor Site for Local Anesthetics *

    Journal: The Journal of Biological Chemistry

    doi: 10.1074/jbc.M113.541763

    Structure of the external access pathway. The proposed molecular arrangement of crucial amino acids involved in access and binding of QX-222 is shown. A and B ), respectively, based
    Figure Legend Snippet: Structure of the external access pathway. The proposed molecular arrangement of crucial amino acids involved in access and binding of QX-222 is shown. A and B ), respectively, based

    Techniques Used: Binding Assay

    Recovery from block by intracellular QX-222. A 5-s-long 10-Hz pulse train was applied for repetitive openings of the channels to bind QX-222 to the inner vestibule. After the last pulse in the train, the cell was repolarized to −140 mV for various
    Figure Legend Snippet: Recovery from block by intracellular QX-222. A 5-s-long 10-Hz pulse train was applied for repetitive openings of the channels to bind QX-222 to the inner vestibule. After the last pulse in the train, the cell was repolarized to −140 mV for various

    Techniques Used: Blocking Assay

    The binding site for external QX-222 is in the internal vestibule. Modulation of the EAP by an additional mutation in the selectivity filter and by mutations of Trp-1531 is shown. The stimulation protocol and depiction are the same as in B. A , residue
    Figure Legend Snippet: The binding site for external QX-222 is in the internal vestibule. Modulation of the EAP by an additional mutation in the selectivity filter and by mutations of Trp-1531 is shown. The stimulation protocol and depiction are the same as in B. A , residue

    Techniques Used: Binding Assay, Mutagenesis

    Mutations at Site 1575 Open an EAP for QX-222
    Figure Legend Snippet: Mutations at Site 1575 Open an EAP for QX-222

    Techniques Used:

    Effect of QX-222 on inactivation properties of channels carrying mutations at site 1531. A , in W1531A, 500 μ m QX-222 significantly shifted the steady-state inactivation curve to hyperpolarized potentials. V 1/2 was −74.6 ± 0.6 and
    Figure Legend Snippet: Effect of QX-222 on inactivation properties of channels carrying mutations at site 1531. A , in W1531A, 500 μ m QX-222 significantly shifted the steady-state inactivation curve to hyperpolarized potentials. V 1/2 was −74.6 ± 0.6 and

    Techniques Used:

    External block by QX-222 is favored by replacement of Ile-1575 with amino acids of small size or with hydrophilic properties. Sodium currents were evoked by depolarizing pulses at a frequency of 2 Hz (see “Experimental Procedures”). Connecting
    Figure Legend Snippet: External block by QX-222 is favored by replacement of Ile-1575 with amino acids of small size or with hydrophilic properties. Sodium currents were evoked by depolarizing pulses at a frequency of 2 Hz (see “Experimental Procedures”). Connecting

    Techniques Used: Blocking Assay

    Use-dependent block by external QX-222. A 2-Hz pulse train was applied for 30 s at a holding potential of −120 mV. Thereafter, external perfusion with QX-222 was started while cells were kept at the holding potential for 120 s. Then repetitive
    Figure Legend Snippet: Use-dependent block by external QX-222. A 2-Hz pulse train was applied for 30 s at a holding potential of −120 mV. Thereafter, external perfusion with QX-222 was started while cells were kept at the holding potential for 120 s. Then repetitive

    Techniques Used: Blocking Assay

    23) Product Images from "Exploring the Structure of the Voltage-gated Na+ Channel by an Engineered Drug Access Pathway to the Receptor Site for Local Anesthetics *"

    Article Title: Exploring the Structure of the Voltage-gated Na+ Channel by an Engineered Drug Access Pathway to the Receptor Site for Local Anesthetics *

    Journal: The Journal of Biological Chemistry

    doi: 10.1074/jbc.M113.541763

    Structure of the external access pathway. The proposed molecular arrangement of crucial amino acids involved in access and binding of QX-222 is shown. A and B ), respectively, based
    Figure Legend Snippet: Structure of the external access pathway. The proposed molecular arrangement of crucial amino acids involved in access and binding of QX-222 is shown. A and B ), respectively, based

    Techniques Used: Binding Assay

    Recovery from block by intracellular QX-222. A 5-s-long 10-Hz pulse train was applied for repetitive openings of the channels to bind QX-222 to the inner vestibule. After the last pulse in the train, the cell was repolarized to −140 mV for various
    Figure Legend Snippet: Recovery from block by intracellular QX-222. A 5-s-long 10-Hz pulse train was applied for repetitive openings of the channels to bind QX-222 to the inner vestibule. After the last pulse in the train, the cell was repolarized to −140 mV for various

    Techniques Used: Blocking Assay

    The binding site for external QX-222 is in the internal vestibule. Modulation of the EAP by an additional mutation in the selectivity filter and by mutations of Trp-1531 is shown. The stimulation protocol and depiction are the same as in B. A , residue
    Figure Legend Snippet: The binding site for external QX-222 is in the internal vestibule. Modulation of the EAP by an additional mutation in the selectivity filter and by mutations of Trp-1531 is shown. The stimulation protocol and depiction are the same as in B. A , residue

    Techniques Used: Binding Assay, Mutagenesis

    Mutations at Site 1575 Open an EAP for QX-222
    Figure Legend Snippet: Mutations at Site 1575 Open an EAP for QX-222

    Techniques Used:

    Effect of QX-222 on inactivation properties of channels carrying mutations at site 1531. A , in W1531A, 500 μ m QX-222 significantly shifted the steady-state inactivation curve to hyperpolarized potentials. V 1/2 was −74.6 ± 0.6 and
    Figure Legend Snippet: Effect of QX-222 on inactivation properties of channels carrying mutations at site 1531. A , in W1531A, 500 μ m QX-222 significantly shifted the steady-state inactivation curve to hyperpolarized potentials. V 1/2 was −74.6 ± 0.6 and

    Techniques Used:

    External block by QX-222 is favored by replacement of Ile-1575 with amino acids of small size or with hydrophilic properties. Sodium currents were evoked by depolarizing pulses at a frequency of 2 Hz (see “Experimental Procedures”). Connecting
    Figure Legend Snippet: External block by QX-222 is favored by replacement of Ile-1575 with amino acids of small size or with hydrophilic properties. Sodium currents were evoked by depolarizing pulses at a frequency of 2 Hz (see “Experimental Procedures”). Connecting

    Techniques Used: Blocking Assay

    Use-dependent block by external QX-222. A 2-Hz pulse train was applied for 30 s at a holding potential of −120 mV. Thereafter, external perfusion with QX-222 was started while cells were kept at the holding potential for 120 s. Then repetitive
    Figure Legend Snippet: Use-dependent block by external QX-222. A 2-Hz pulse train was applied for 30 s at a holding potential of −120 mV. Thereafter, external perfusion with QX-222 was started while cells were kept at the holding potential for 120 s. Then repetitive

    Techniques Used: Blocking Assay

    24) Product Images from "Exploring the Structure of the Voltage-gated Na+ Channel by an Engineered Drug Access Pathway to the Receptor Site for Local Anesthetics *"

    Article Title: Exploring the Structure of the Voltage-gated Na+ Channel by an Engineered Drug Access Pathway to the Receptor Site for Local Anesthetics *

    Journal: The Journal of Biological Chemistry

    doi: 10.1074/jbc.M113.541763

    Structure of the external access pathway. The proposed molecular arrangement of crucial amino acids involved in access and binding of QX-222 is shown. A and B ), respectively, based
    Figure Legend Snippet: Structure of the external access pathway. The proposed molecular arrangement of crucial amino acids involved in access and binding of QX-222 is shown. A and B ), respectively, based

    Techniques Used: Binding Assay

    Recovery from block by intracellular QX-222. A 5-s-long 10-Hz pulse train was applied for repetitive openings of the channels to bind QX-222 to the inner vestibule. After the last pulse in the train, the cell was repolarized to −140 mV for various
    Figure Legend Snippet: Recovery from block by intracellular QX-222. A 5-s-long 10-Hz pulse train was applied for repetitive openings of the channels to bind QX-222 to the inner vestibule. After the last pulse in the train, the cell was repolarized to −140 mV for various

    Techniques Used: Blocking Assay

    The binding site for external QX-222 is in the internal vestibule. Modulation of the EAP by an additional mutation in the selectivity filter and by mutations of Trp-1531 is shown. The stimulation protocol and depiction are the same as in B. A , residue
    Figure Legend Snippet: The binding site for external QX-222 is in the internal vestibule. Modulation of the EAP by an additional mutation in the selectivity filter and by mutations of Trp-1531 is shown. The stimulation protocol and depiction are the same as in B. A , residue

    Techniques Used: Binding Assay, Mutagenesis

    Mutations at Site 1575 Open an EAP for QX-222
    Figure Legend Snippet: Mutations at Site 1575 Open an EAP for QX-222

    Techniques Used:

    Effect of QX-222 on inactivation properties of channels carrying mutations at site 1531. A , in W1531A, 500 μ m QX-222 significantly shifted the steady-state inactivation curve to hyperpolarized potentials. V 1/2 was −74.6 ± 0.6 and
    Figure Legend Snippet: Effect of QX-222 on inactivation properties of channels carrying mutations at site 1531. A , in W1531A, 500 μ m QX-222 significantly shifted the steady-state inactivation curve to hyperpolarized potentials. V 1/2 was −74.6 ± 0.6 and

    Techniques Used:

    External block by QX-222 is favored by replacement of Ile-1575 with amino acids of small size or with hydrophilic properties. Sodium currents were evoked by depolarizing pulses at a frequency of 2 Hz (see “Experimental Procedures”). Connecting
    Figure Legend Snippet: External block by QX-222 is favored by replacement of Ile-1575 with amino acids of small size or with hydrophilic properties. Sodium currents were evoked by depolarizing pulses at a frequency of 2 Hz (see “Experimental Procedures”). Connecting

    Techniques Used: Blocking Assay

    Use-dependent block by external QX-222. A 2-Hz pulse train was applied for 30 s at a holding potential of −120 mV. Thereafter, external perfusion with QX-222 was started while cells were kept at the holding potential for 120 s. Then repetitive
    Figure Legend Snippet: Use-dependent block by external QX-222. A 2-Hz pulse train was applied for 30 s at a holding potential of −120 mV. Thereafter, external perfusion with QX-222 was started while cells were kept at the holding potential for 120 s. Then repetitive

    Techniques Used: Blocking Assay

    25) Product Images from "Exploring the Structure of the Voltage-gated Na+ Channel by an Engineered Drug Access Pathway to the Receptor Site for Local Anesthetics *"

    Article Title: Exploring the Structure of the Voltage-gated Na+ Channel by an Engineered Drug Access Pathway to the Receptor Site for Local Anesthetics *

    Journal: The Journal of Biological Chemistry

    doi: 10.1074/jbc.M113.541763

    Structure of the external access pathway. The proposed molecular arrangement of crucial amino acids involved in access and binding of QX-222 is shown. A and B ), respectively, based
    Figure Legend Snippet: Structure of the external access pathway. The proposed molecular arrangement of crucial amino acids involved in access and binding of QX-222 is shown. A and B ), respectively, based

    Techniques Used: Binding Assay

    Recovery from block by intracellular QX-222. A 5-s-long 10-Hz pulse train was applied for repetitive openings of the channels to bind QX-222 to the inner vestibule. After the last pulse in the train, the cell was repolarized to −140 mV for various
    Figure Legend Snippet: Recovery from block by intracellular QX-222. A 5-s-long 10-Hz pulse train was applied for repetitive openings of the channels to bind QX-222 to the inner vestibule. After the last pulse in the train, the cell was repolarized to −140 mV for various

    Techniques Used: Blocking Assay

    The binding site for external QX-222 is in the internal vestibule. Modulation of the EAP by an additional mutation in the selectivity filter and by mutations of Trp-1531 is shown. The stimulation protocol and depiction are the same as in B. A , residue
    Figure Legend Snippet: The binding site for external QX-222 is in the internal vestibule. Modulation of the EAP by an additional mutation in the selectivity filter and by mutations of Trp-1531 is shown. The stimulation protocol and depiction are the same as in B. A , residue

    Techniques Used: Binding Assay, Mutagenesis

    Mutations at Site 1575 Open an EAP for QX-222
    Figure Legend Snippet: Mutations at Site 1575 Open an EAP for QX-222

    Techniques Used:

    Effect of QX-222 on inactivation properties of channels carrying mutations at site 1531. A , in W1531A, 500 μ m QX-222 significantly shifted the steady-state inactivation curve to hyperpolarized potentials. V 1/2 was −74.6 ± 0.6 and
    Figure Legend Snippet: Effect of QX-222 on inactivation properties of channels carrying mutations at site 1531. A , in W1531A, 500 μ m QX-222 significantly shifted the steady-state inactivation curve to hyperpolarized potentials. V 1/2 was −74.6 ± 0.6 and

    Techniques Used:

    External block by QX-222 is favored by replacement of Ile-1575 with amino acids of small size or with hydrophilic properties. Sodium currents were evoked by depolarizing pulses at a frequency of 2 Hz (see “Experimental Procedures”). Connecting
    Figure Legend Snippet: External block by QX-222 is favored by replacement of Ile-1575 with amino acids of small size or with hydrophilic properties. Sodium currents were evoked by depolarizing pulses at a frequency of 2 Hz (see “Experimental Procedures”). Connecting

    Techniques Used: Blocking Assay

    Use-dependent block by external QX-222. A 2-Hz pulse train was applied for 30 s at a holding potential of −120 mV. Thereafter, external perfusion with QX-222 was started while cells were kept at the holding potential for 120 s. Then repetitive
    Figure Legend Snippet: Use-dependent block by external QX-222. A 2-Hz pulse train was applied for 30 s at a holding potential of −120 mV. Thereafter, external perfusion with QX-222 was started while cells were kept at the holding potential for 120 s. Then repetitive

    Techniques Used: Blocking Assay

    26) Product Images from "Exploring the Structure of the Voltage-gated Na+ Channel by an Engineered Drug Access Pathway to the Receptor Site for Local Anesthetics *"

    Article Title: Exploring the Structure of the Voltage-gated Na+ Channel by an Engineered Drug Access Pathway to the Receptor Site for Local Anesthetics *

    Journal: The Journal of Biological Chemistry

    doi: 10.1074/jbc.M113.541763

    Structure of the external access pathway. The proposed molecular arrangement of crucial amino acids involved in access and binding of QX-222 is shown. A and B ), respectively, based
    Figure Legend Snippet: Structure of the external access pathway. The proposed molecular arrangement of crucial amino acids involved in access and binding of QX-222 is shown. A and B ), respectively, based

    Techniques Used: Binding Assay

    Recovery from block by intracellular QX-222. A 5-s-long 10-Hz pulse train was applied for repetitive openings of the channels to bind QX-222 to the inner vestibule. After the last pulse in the train, the cell was repolarized to −140 mV for various
    Figure Legend Snippet: Recovery from block by intracellular QX-222. A 5-s-long 10-Hz pulse train was applied for repetitive openings of the channels to bind QX-222 to the inner vestibule. After the last pulse in the train, the cell was repolarized to −140 mV for various

    Techniques Used: Blocking Assay

    The binding site for external QX-222 is in the internal vestibule. Modulation of the EAP by an additional mutation in the selectivity filter and by mutations of Trp-1531 is shown. The stimulation protocol and depiction are the same as in B. A , residue
    Figure Legend Snippet: The binding site for external QX-222 is in the internal vestibule. Modulation of the EAP by an additional mutation in the selectivity filter and by mutations of Trp-1531 is shown. The stimulation protocol and depiction are the same as in B. A , residue

    Techniques Used: Binding Assay, Mutagenesis

    Mutations at Site 1575 Open an EAP for QX-222
    Figure Legend Snippet: Mutations at Site 1575 Open an EAP for QX-222

    Techniques Used:

    Effect of QX-222 on inactivation properties of channels carrying mutations at site 1531. A , in W1531A, 500 μ m QX-222 significantly shifted the steady-state inactivation curve to hyperpolarized potentials. V 1/2 was −74.6 ± 0.6 and
    Figure Legend Snippet: Effect of QX-222 on inactivation properties of channels carrying mutations at site 1531. A , in W1531A, 500 μ m QX-222 significantly shifted the steady-state inactivation curve to hyperpolarized potentials. V 1/2 was −74.6 ± 0.6 and

    Techniques Used:

    External block by QX-222 is favored by replacement of Ile-1575 with amino acids of small size or with hydrophilic properties. Sodium currents were evoked by depolarizing pulses at a frequency of 2 Hz (see “Experimental Procedures”). Connecting
    Figure Legend Snippet: External block by QX-222 is favored by replacement of Ile-1575 with amino acids of small size or with hydrophilic properties. Sodium currents were evoked by depolarizing pulses at a frequency of 2 Hz (see “Experimental Procedures”). Connecting

    Techniques Used: Blocking Assay

    Use-dependent block by external QX-222. A 2-Hz pulse train was applied for 30 s at a holding potential of −120 mV. Thereafter, external perfusion with QX-222 was started while cells were kept at the holding potential for 120 s. Then repetitive
    Figure Legend Snippet: Use-dependent block by external QX-222. A 2-Hz pulse train was applied for 30 s at a holding potential of −120 mV. Thereafter, external perfusion with QX-222 was started while cells were kept at the holding potential for 120 s. Then repetitive

    Techniques Used: Blocking Assay

    27) Product Images from "Exploring the Structure of the Voltage-gated Na+ Channel by an Engineered Drug Access Pathway to the Receptor Site for Local Anesthetics *"

    Article Title: Exploring the Structure of the Voltage-gated Na+ Channel by an Engineered Drug Access Pathway to the Receptor Site for Local Anesthetics *

    Journal: The Journal of Biological Chemistry

    doi: 10.1074/jbc.M113.541763

    Structure of the external access pathway. The proposed molecular arrangement of crucial amino acids involved in access and binding of QX-222 is shown. A and B ), respectively, based
    Figure Legend Snippet: Structure of the external access pathway. The proposed molecular arrangement of crucial amino acids involved in access and binding of QX-222 is shown. A and B ), respectively, based

    Techniques Used: Binding Assay

    Recovery from block by intracellular QX-222. A 5-s-long 10-Hz pulse train was applied for repetitive openings of the channels to bind QX-222 to the inner vestibule. After the last pulse in the train, the cell was repolarized to −140 mV for various
    Figure Legend Snippet: Recovery from block by intracellular QX-222. A 5-s-long 10-Hz pulse train was applied for repetitive openings of the channels to bind QX-222 to the inner vestibule. After the last pulse in the train, the cell was repolarized to −140 mV for various

    Techniques Used: Blocking Assay

    The binding site for external QX-222 is in the internal vestibule. Modulation of the EAP by an additional mutation in the selectivity filter and by mutations of Trp-1531 is shown. The stimulation protocol and depiction are the same as in B. A , residue
    Figure Legend Snippet: The binding site for external QX-222 is in the internal vestibule. Modulation of the EAP by an additional mutation in the selectivity filter and by mutations of Trp-1531 is shown. The stimulation protocol and depiction are the same as in B. A , residue

    Techniques Used: Binding Assay, Mutagenesis

    Mutations at Site 1575 Open an EAP for QX-222
    Figure Legend Snippet: Mutations at Site 1575 Open an EAP for QX-222

    Techniques Used:

    Effect of QX-222 on inactivation properties of channels carrying mutations at site 1531. A , in W1531A, 500 μ m QX-222 significantly shifted the steady-state inactivation curve to hyperpolarized potentials. V 1/2 was −74.6 ± 0.6 and
    Figure Legend Snippet: Effect of QX-222 on inactivation properties of channels carrying mutations at site 1531. A , in W1531A, 500 μ m QX-222 significantly shifted the steady-state inactivation curve to hyperpolarized potentials. V 1/2 was −74.6 ± 0.6 and

    Techniques Used:

    External block by QX-222 is favored by replacement of Ile-1575 with amino acids of small size or with hydrophilic properties. Sodium currents were evoked by depolarizing pulses at a frequency of 2 Hz (see “Experimental Procedures”). Connecting
    Figure Legend Snippet: External block by QX-222 is favored by replacement of Ile-1575 with amino acids of small size or with hydrophilic properties. Sodium currents were evoked by depolarizing pulses at a frequency of 2 Hz (see “Experimental Procedures”). Connecting

    Techniques Used: Blocking Assay

    Use-dependent block by external QX-222. A 2-Hz pulse train was applied for 30 s at a holding potential of −120 mV. Thereafter, external perfusion with QX-222 was started while cells were kept at the holding potential for 120 s. Then repetitive
    Figure Legend Snippet: Use-dependent block by external QX-222. A 2-Hz pulse train was applied for 30 s at a holding potential of −120 mV. Thereafter, external perfusion with QX-222 was started while cells were kept at the holding potential for 120 s. Then repetitive

    Techniques Used: Blocking Assay

    28) Product Images from "Exploring the Structure of the Voltage-gated Na+ Channel by an Engineered Drug Access Pathway to the Receptor Site for Local Anesthetics *"

    Article Title: Exploring the Structure of the Voltage-gated Na+ Channel by an Engineered Drug Access Pathway to the Receptor Site for Local Anesthetics *

    Journal: The Journal of Biological Chemistry

    doi: 10.1074/jbc.M113.541763

    Structure of the external access pathway. The proposed molecular arrangement of crucial amino acids involved in access and binding of QX-222 is shown. A and B ), respectively, based
    Figure Legend Snippet: Structure of the external access pathway. The proposed molecular arrangement of crucial amino acids involved in access and binding of QX-222 is shown. A and B ), respectively, based

    Techniques Used: Binding Assay

    Recovery from block by intracellular QX-222. A 5-s-long 10-Hz pulse train was applied for repetitive openings of the channels to bind QX-222 to the inner vestibule. After the last pulse in the train, the cell was repolarized to −140 mV for various
    Figure Legend Snippet: Recovery from block by intracellular QX-222. A 5-s-long 10-Hz pulse train was applied for repetitive openings of the channels to bind QX-222 to the inner vestibule. After the last pulse in the train, the cell was repolarized to −140 mV for various

    Techniques Used: Blocking Assay

    The binding site for external QX-222 is in the internal vestibule. Modulation of the EAP by an additional mutation in the selectivity filter and by mutations of Trp-1531 is shown. The stimulation protocol and depiction are the same as in B. A , residue
    Figure Legend Snippet: The binding site for external QX-222 is in the internal vestibule. Modulation of the EAP by an additional mutation in the selectivity filter and by mutations of Trp-1531 is shown. The stimulation protocol and depiction are the same as in B. A , residue

    Techniques Used: Binding Assay, Mutagenesis

    Mutations at Site 1575 Open an EAP for QX-222
    Figure Legend Snippet: Mutations at Site 1575 Open an EAP for QX-222

    Techniques Used:

    Effect of QX-222 on inactivation properties of channels carrying mutations at site 1531. A , in W1531A, 500 μ m QX-222 significantly shifted the steady-state inactivation curve to hyperpolarized potentials. V 1/2 was −74.6 ± 0.6 and
    Figure Legend Snippet: Effect of QX-222 on inactivation properties of channels carrying mutations at site 1531. A , in W1531A, 500 μ m QX-222 significantly shifted the steady-state inactivation curve to hyperpolarized potentials. V 1/2 was −74.6 ± 0.6 and

    Techniques Used:

    External block by QX-222 is favored by replacement of Ile-1575 with amino acids of small size or with hydrophilic properties. Sodium currents were evoked by depolarizing pulses at a frequency of 2 Hz (see “Experimental Procedures”). Connecting
    Figure Legend Snippet: External block by QX-222 is favored by replacement of Ile-1575 with amino acids of small size or with hydrophilic properties. Sodium currents were evoked by depolarizing pulses at a frequency of 2 Hz (see “Experimental Procedures”). Connecting

    Techniques Used: Blocking Assay

    Use-dependent block by external QX-222. A 2-Hz pulse train was applied for 30 s at a holding potential of −120 mV. Thereafter, external perfusion with QX-222 was started while cells were kept at the holding potential for 120 s. Then repetitive
    Figure Legend Snippet: Use-dependent block by external QX-222. A 2-Hz pulse train was applied for 30 s at a holding potential of −120 mV. Thereafter, external perfusion with QX-222 was started while cells were kept at the holding potential for 120 s. Then repetitive

    Techniques Used: Blocking Assay

    29) Product Images from "Exploring the Structure of the Voltage-gated Na+ Channel by an Engineered Drug Access Pathway to the Receptor Site for Local Anesthetics *"

    Article Title: Exploring the Structure of the Voltage-gated Na+ Channel by an Engineered Drug Access Pathway to the Receptor Site for Local Anesthetics *

    Journal: The Journal of Biological Chemistry

    doi: 10.1074/jbc.M113.541763

    Structure of the external access pathway. The proposed molecular arrangement of crucial amino acids involved in access and binding of QX-222 is shown. A and B ), respectively, based
    Figure Legend Snippet: Structure of the external access pathway. The proposed molecular arrangement of crucial amino acids involved in access and binding of QX-222 is shown. A and B ), respectively, based

    Techniques Used: Binding Assay

    Recovery from block by intracellular QX-222. A 5-s-long 10-Hz pulse train was applied for repetitive openings of the channels to bind QX-222 to the inner vestibule. After the last pulse in the train, the cell was repolarized to −140 mV for various
    Figure Legend Snippet: Recovery from block by intracellular QX-222. A 5-s-long 10-Hz pulse train was applied for repetitive openings of the channels to bind QX-222 to the inner vestibule. After the last pulse in the train, the cell was repolarized to −140 mV for various

    Techniques Used: Blocking Assay

    The binding site for external QX-222 is in the internal vestibule. Modulation of the EAP by an additional mutation in the selectivity filter and by mutations of Trp-1531 is shown. The stimulation protocol and depiction are the same as in B. A , residue
    Figure Legend Snippet: The binding site for external QX-222 is in the internal vestibule. Modulation of the EAP by an additional mutation in the selectivity filter and by mutations of Trp-1531 is shown. The stimulation protocol and depiction are the same as in B. A , residue

    Techniques Used: Binding Assay, Mutagenesis

    Mutations at Site 1575 Open an EAP for QX-222
    Figure Legend Snippet: Mutations at Site 1575 Open an EAP for QX-222

    Techniques Used:

    Effect of QX-222 on inactivation properties of channels carrying mutations at site 1531. A , in W1531A, 500 μ m QX-222 significantly shifted the steady-state inactivation curve to hyperpolarized potentials. V 1/2 was −74.6 ± 0.6 and
    Figure Legend Snippet: Effect of QX-222 on inactivation properties of channels carrying mutations at site 1531. A , in W1531A, 500 μ m QX-222 significantly shifted the steady-state inactivation curve to hyperpolarized potentials. V 1/2 was −74.6 ± 0.6 and

    Techniques Used:

    External block by QX-222 is favored by replacement of Ile-1575 with amino acids of small size or with hydrophilic properties. Sodium currents were evoked by depolarizing pulses at a frequency of 2 Hz (see “Experimental Procedures”). Connecting
    Figure Legend Snippet: External block by QX-222 is favored by replacement of Ile-1575 with amino acids of small size or with hydrophilic properties. Sodium currents were evoked by depolarizing pulses at a frequency of 2 Hz (see “Experimental Procedures”). Connecting

    Techniques Used: Blocking Assay

    Use-dependent block by external QX-222. A 2-Hz pulse train was applied for 30 s at a holding potential of −120 mV. Thereafter, external perfusion with QX-222 was started while cells were kept at the holding potential for 120 s. Then repetitive
    Figure Legend Snippet: Use-dependent block by external QX-222. A 2-Hz pulse train was applied for 30 s at a holding potential of −120 mV. Thereafter, external perfusion with QX-222 was started while cells were kept at the holding potential for 120 s. Then repetitive

    Techniques Used: Blocking Assay

    30) Product Images from "Exploring the Structure of the Voltage-gated Na+ Channel by an Engineered Drug Access Pathway to the Receptor Site for Local Anesthetics *"

    Article Title: Exploring the Structure of the Voltage-gated Na+ Channel by an Engineered Drug Access Pathway to the Receptor Site for Local Anesthetics *

    Journal: The Journal of Biological Chemistry

    doi: 10.1074/jbc.M113.541763

    Structure of the external access pathway. The proposed molecular arrangement of crucial amino acids involved in access and binding of QX-222 is shown. A and B ), respectively, based
    Figure Legend Snippet: Structure of the external access pathway. The proposed molecular arrangement of crucial amino acids involved in access and binding of QX-222 is shown. A and B ), respectively, based

    Techniques Used: Binding Assay

    Recovery from block by intracellular QX-222. A 5-s-long 10-Hz pulse train was applied for repetitive openings of the channels to bind QX-222 to the inner vestibule. After the last pulse in the train, the cell was repolarized to −140 mV for various
    Figure Legend Snippet: Recovery from block by intracellular QX-222. A 5-s-long 10-Hz pulse train was applied for repetitive openings of the channels to bind QX-222 to the inner vestibule. After the last pulse in the train, the cell was repolarized to −140 mV for various

    Techniques Used: Blocking Assay

    The binding site for external QX-222 is in the internal vestibule. Modulation of the EAP by an additional mutation in the selectivity filter and by mutations of Trp-1531 is shown. The stimulation protocol and depiction are the same as in B. A , residue
    Figure Legend Snippet: The binding site for external QX-222 is in the internal vestibule. Modulation of the EAP by an additional mutation in the selectivity filter and by mutations of Trp-1531 is shown. The stimulation protocol and depiction are the same as in B. A , residue

    Techniques Used: Binding Assay, Mutagenesis

    Mutations at Site 1575 Open an EAP for QX-222
    Figure Legend Snippet: Mutations at Site 1575 Open an EAP for QX-222

    Techniques Used:

    Effect of QX-222 on inactivation properties of channels carrying mutations at site 1531. A , in W1531A, 500 μ m QX-222 significantly shifted the steady-state inactivation curve to hyperpolarized potentials. V 1/2 was −74.6 ± 0.6 and
    Figure Legend Snippet: Effect of QX-222 on inactivation properties of channels carrying mutations at site 1531. A , in W1531A, 500 μ m QX-222 significantly shifted the steady-state inactivation curve to hyperpolarized potentials. V 1/2 was −74.6 ± 0.6 and

    Techniques Used:

    External block by QX-222 is favored by replacement of Ile-1575 with amino acids of small size or with hydrophilic properties. Sodium currents were evoked by depolarizing pulses at a frequency of 2 Hz (see “Experimental Procedures”). Connecting
    Figure Legend Snippet: External block by QX-222 is favored by replacement of Ile-1575 with amino acids of small size or with hydrophilic properties. Sodium currents were evoked by depolarizing pulses at a frequency of 2 Hz (see “Experimental Procedures”). Connecting

    Techniques Used: Blocking Assay

    Use-dependent block by external QX-222. A 2-Hz pulse train was applied for 30 s at a holding potential of −120 mV. Thereafter, external perfusion with QX-222 was started while cells were kept at the holding potential for 120 s. Then repetitive
    Figure Legend Snippet: Use-dependent block by external QX-222. A 2-Hz pulse train was applied for 30 s at a holding potential of −120 mV. Thereafter, external perfusion with QX-222 was started while cells were kept at the holding potential for 120 s. Then repetitive

    Techniques Used: Blocking Assay

    31) Product Images from "Exploring the Structure of the Voltage-gated Na+ Channel by an Engineered Drug Access Pathway to the Receptor Site for Local Anesthetics *"

    Article Title: Exploring the Structure of the Voltage-gated Na+ Channel by an Engineered Drug Access Pathway to the Receptor Site for Local Anesthetics *

    Journal: The Journal of Biological Chemistry

    doi: 10.1074/jbc.M113.541763

    Structure of the external access pathway. The proposed molecular arrangement of crucial amino acids involved in access and binding of QX-222 is shown. A and B ), respectively, based
    Figure Legend Snippet: Structure of the external access pathway. The proposed molecular arrangement of crucial amino acids involved in access and binding of QX-222 is shown. A and B ), respectively, based

    Techniques Used: Binding Assay

    Recovery from block by intracellular QX-222. A 5-s-long 10-Hz pulse train was applied for repetitive openings of the channels to bind QX-222 to the inner vestibule. After the last pulse in the train, the cell was repolarized to −140 mV for various
    Figure Legend Snippet: Recovery from block by intracellular QX-222. A 5-s-long 10-Hz pulse train was applied for repetitive openings of the channels to bind QX-222 to the inner vestibule. After the last pulse in the train, the cell was repolarized to −140 mV for various

    Techniques Used: Blocking Assay

    The binding site for external QX-222 is in the internal vestibule. Modulation of the EAP by an additional mutation in the selectivity filter and by mutations of Trp-1531 is shown. The stimulation protocol and depiction are the same as in B. A , residue
    Figure Legend Snippet: The binding site for external QX-222 is in the internal vestibule. Modulation of the EAP by an additional mutation in the selectivity filter and by mutations of Trp-1531 is shown. The stimulation protocol and depiction are the same as in B. A , residue

    Techniques Used: Binding Assay, Mutagenesis

    Mutations at Site 1575 Open an EAP for QX-222
    Figure Legend Snippet: Mutations at Site 1575 Open an EAP for QX-222

    Techniques Used:

    Effect of QX-222 on inactivation properties of channels carrying mutations at site 1531. A , in W1531A, 500 μ m QX-222 significantly shifted the steady-state inactivation curve to hyperpolarized potentials. V 1/2 was −74.6 ± 0.6 and
    Figure Legend Snippet: Effect of QX-222 on inactivation properties of channels carrying mutations at site 1531. A , in W1531A, 500 μ m QX-222 significantly shifted the steady-state inactivation curve to hyperpolarized potentials. V 1/2 was −74.6 ± 0.6 and

    Techniques Used:

    External block by QX-222 is favored by replacement of Ile-1575 with amino acids of small size or with hydrophilic properties. Sodium currents were evoked by depolarizing pulses at a frequency of 2 Hz (see “Experimental Procedures”). Connecting
    Figure Legend Snippet: External block by QX-222 is favored by replacement of Ile-1575 with amino acids of small size or with hydrophilic properties. Sodium currents were evoked by depolarizing pulses at a frequency of 2 Hz (see “Experimental Procedures”). Connecting

    Techniques Used: Blocking Assay

    Use-dependent block by external QX-222. A 2-Hz pulse train was applied for 30 s at a holding potential of −120 mV. Thereafter, external perfusion with QX-222 was started while cells were kept at the holding potential for 120 s. Then repetitive
    Figure Legend Snippet: Use-dependent block by external QX-222. A 2-Hz pulse train was applied for 30 s at a holding potential of −120 mV. Thereafter, external perfusion with QX-222 was started while cells were kept at the holding potential for 120 s. Then repetitive

    Techniques Used: Blocking Assay

    32) Product Images from "Exploring the Structure of the Voltage-gated Na+ Channel by an Engineered Drug Access Pathway to the Receptor Site for Local Anesthetics *"

    Article Title: Exploring the Structure of the Voltage-gated Na+ Channel by an Engineered Drug Access Pathway to the Receptor Site for Local Anesthetics *

    Journal: The Journal of Biological Chemistry

    doi: 10.1074/jbc.M113.541763

    Structure of the external access pathway. The proposed molecular arrangement of crucial amino acids involved in access and binding of QX-222 is shown. A and B ), respectively, based
    Figure Legend Snippet: Structure of the external access pathway. The proposed molecular arrangement of crucial amino acids involved in access and binding of QX-222 is shown. A and B ), respectively, based

    Techniques Used: Binding Assay

    Recovery from block by intracellular QX-222. A 5-s-long 10-Hz pulse train was applied for repetitive openings of the channels to bind QX-222 to the inner vestibule. After the last pulse in the train, the cell was repolarized to −140 mV for various
    Figure Legend Snippet: Recovery from block by intracellular QX-222. A 5-s-long 10-Hz pulse train was applied for repetitive openings of the channels to bind QX-222 to the inner vestibule. After the last pulse in the train, the cell was repolarized to −140 mV for various

    Techniques Used: Blocking Assay

    The binding site for external QX-222 is in the internal vestibule. Modulation of the EAP by an additional mutation in the selectivity filter and by mutations of Trp-1531 is shown. The stimulation protocol and depiction are the same as in B. A , residue
    Figure Legend Snippet: The binding site for external QX-222 is in the internal vestibule. Modulation of the EAP by an additional mutation in the selectivity filter and by mutations of Trp-1531 is shown. The stimulation protocol and depiction are the same as in B. A , residue

    Techniques Used: Binding Assay, Mutagenesis

    Mutations at Site 1575 Open an EAP for QX-222
    Figure Legend Snippet: Mutations at Site 1575 Open an EAP for QX-222

    Techniques Used:

    Effect of QX-222 on inactivation properties of channels carrying mutations at site 1531. A , in W1531A, 500 μ m QX-222 significantly shifted the steady-state inactivation curve to hyperpolarized potentials. V 1/2 was −74.6 ± 0.6 and
    Figure Legend Snippet: Effect of QX-222 on inactivation properties of channels carrying mutations at site 1531. A , in W1531A, 500 μ m QX-222 significantly shifted the steady-state inactivation curve to hyperpolarized potentials. V 1/2 was −74.6 ± 0.6 and

    Techniques Used:

    External block by QX-222 is favored by replacement of Ile-1575 with amino acids of small size or with hydrophilic properties. Sodium currents were evoked by depolarizing pulses at a frequency of 2 Hz (see “Experimental Procedures”). Connecting
    Figure Legend Snippet: External block by QX-222 is favored by replacement of Ile-1575 with amino acids of small size or with hydrophilic properties. Sodium currents were evoked by depolarizing pulses at a frequency of 2 Hz (see “Experimental Procedures”). Connecting

    Techniques Used: Blocking Assay

    Use-dependent block by external QX-222. A 2-Hz pulse train was applied for 30 s at a holding potential of −120 mV. Thereafter, external perfusion with QX-222 was started while cells were kept at the holding potential for 120 s. Then repetitive
    Figure Legend Snippet: Use-dependent block by external QX-222. A 2-Hz pulse train was applied for 30 s at a holding potential of −120 mV. Thereafter, external perfusion with QX-222 was started while cells were kept at the holding potential for 120 s. Then repetitive

    Techniques Used: Blocking Assay

    33) Product Images from "Exploring the Structure of the Voltage-gated Na+ Channel by an Engineered Drug Access Pathway to the Receptor Site for Local Anesthetics *"

    Article Title: Exploring the Structure of the Voltage-gated Na+ Channel by an Engineered Drug Access Pathway to the Receptor Site for Local Anesthetics *

    Journal: The Journal of Biological Chemistry

    doi: 10.1074/jbc.M113.541763

    Structure of the external access pathway. The proposed molecular arrangement of crucial amino acids involved in access and binding of QX-222 is shown. A and B ), respectively, based
    Figure Legend Snippet: Structure of the external access pathway. The proposed molecular arrangement of crucial amino acids involved in access and binding of QX-222 is shown. A and B ), respectively, based

    Techniques Used: Binding Assay

    Recovery from block by intracellular QX-222. A 5-s-long 10-Hz pulse train was applied for repetitive openings of the channels to bind QX-222 to the inner vestibule. After the last pulse in the train, the cell was repolarized to −140 mV for various
    Figure Legend Snippet: Recovery from block by intracellular QX-222. A 5-s-long 10-Hz pulse train was applied for repetitive openings of the channels to bind QX-222 to the inner vestibule. After the last pulse in the train, the cell was repolarized to −140 mV for various

    Techniques Used: Blocking Assay

    The binding site for external QX-222 is in the internal vestibule. Modulation of the EAP by an additional mutation in the selectivity filter and by mutations of Trp-1531 is shown. The stimulation protocol and depiction are the same as in B. A , residue
    Figure Legend Snippet: The binding site for external QX-222 is in the internal vestibule. Modulation of the EAP by an additional mutation in the selectivity filter and by mutations of Trp-1531 is shown. The stimulation protocol and depiction are the same as in B. A , residue

    Techniques Used: Binding Assay, Mutagenesis

    Mutations at Site 1575 Open an EAP for QX-222
    Figure Legend Snippet: Mutations at Site 1575 Open an EAP for QX-222

    Techniques Used:

    Effect of QX-222 on inactivation properties of channels carrying mutations at site 1531. A , in W1531A, 500 μ m QX-222 significantly shifted the steady-state inactivation curve to hyperpolarized potentials. V 1/2 was −74.6 ± 0.6 and
    Figure Legend Snippet: Effect of QX-222 on inactivation properties of channels carrying mutations at site 1531. A , in W1531A, 500 μ m QX-222 significantly shifted the steady-state inactivation curve to hyperpolarized potentials. V 1/2 was −74.6 ± 0.6 and

    Techniques Used:

    External block by QX-222 is favored by replacement of Ile-1575 with amino acids of small size or with hydrophilic properties. Sodium currents were evoked by depolarizing pulses at a frequency of 2 Hz (see “Experimental Procedures”). Connecting
    Figure Legend Snippet: External block by QX-222 is favored by replacement of Ile-1575 with amino acids of small size or with hydrophilic properties. Sodium currents were evoked by depolarizing pulses at a frequency of 2 Hz (see “Experimental Procedures”). Connecting

    Techniques Used: Blocking Assay

    Use-dependent block by external QX-222. A 2-Hz pulse train was applied for 30 s at a holding potential of −120 mV. Thereafter, external perfusion with QX-222 was started while cells were kept at the holding potential for 120 s. Then repetitive
    Figure Legend Snippet: Use-dependent block by external QX-222. A 2-Hz pulse train was applied for 30 s at a holding potential of −120 mV. Thereafter, external perfusion with QX-222 was started while cells were kept at the holding potential for 120 s. Then repetitive

    Techniques Used: Blocking Assay

    34) Product Images from "Exploring the Structure of the Voltage-gated Na+ Channel by an Engineered Drug Access Pathway to the Receptor Site for Local Anesthetics *"

    Article Title: Exploring the Structure of the Voltage-gated Na+ Channel by an Engineered Drug Access Pathway to the Receptor Site for Local Anesthetics *

    Journal: The Journal of Biological Chemistry

    doi: 10.1074/jbc.M113.541763

    Structure of the external access pathway. The proposed molecular arrangement of crucial amino acids involved in access and binding of QX-222 is shown. A and B ), respectively, based
    Figure Legend Snippet: Structure of the external access pathway. The proposed molecular arrangement of crucial amino acids involved in access and binding of QX-222 is shown. A and B ), respectively, based

    Techniques Used: Binding Assay

    Recovery from block by intracellular QX-222. A 5-s-long 10-Hz pulse train was applied for repetitive openings of the channels to bind QX-222 to the inner vestibule. After the last pulse in the train, the cell was repolarized to −140 mV for various
    Figure Legend Snippet: Recovery from block by intracellular QX-222. A 5-s-long 10-Hz pulse train was applied for repetitive openings of the channels to bind QX-222 to the inner vestibule. After the last pulse in the train, the cell was repolarized to −140 mV for various

    Techniques Used: Blocking Assay

    The binding site for external QX-222 is in the internal vestibule. Modulation of the EAP by an additional mutation in the selectivity filter and by mutations of Trp-1531 is shown. The stimulation protocol and depiction are the same as in B. A , residue
    Figure Legend Snippet: The binding site for external QX-222 is in the internal vestibule. Modulation of the EAP by an additional mutation in the selectivity filter and by mutations of Trp-1531 is shown. The stimulation protocol and depiction are the same as in B. A , residue

    Techniques Used: Binding Assay, Mutagenesis

    Mutations at Site 1575 Open an EAP for QX-222
    Figure Legend Snippet: Mutations at Site 1575 Open an EAP for QX-222

    Techniques Used:

    Effect of QX-222 on inactivation properties of channels carrying mutations at site 1531. A , in W1531A, 500 μ m QX-222 significantly shifted the steady-state inactivation curve to hyperpolarized potentials. V 1/2 was −74.6 ± 0.6 and
    Figure Legend Snippet: Effect of QX-222 on inactivation properties of channels carrying mutations at site 1531. A , in W1531A, 500 μ m QX-222 significantly shifted the steady-state inactivation curve to hyperpolarized potentials. V 1/2 was −74.6 ± 0.6 and

    Techniques Used:

    External block by QX-222 is favored by replacement of Ile-1575 with amino acids of small size or with hydrophilic properties. Sodium currents were evoked by depolarizing pulses at a frequency of 2 Hz (see “Experimental Procedures”). Connecting
    Figure Legend Snippet: External block by QX-222 is favored by replacement of Ile-1575 with amino acids of small size or with hydrophilic properties. Sodium currents were evoked by depolarizing pulses at a frequency of 2 Hz (see “Experimental Procedures”). Connecting

    Techniques Used: Blocking Assay

    Use-dependent block by external QX-222. A 2-Hz pulse train was applied for 30 s at a holding potential of −120 mV. Thereafter, external perfusion with QX-222 was started while cells were kept at the holding potential for 120 s. Then repetitive
    Figure Legend Snippet: Use-dependent block by external QX-222. A 2-Hz pulse train was applied for 30 s at a holding potential of −120 mV. Thereafter, external perfusion with QX-222 was started while cells were kept at the holding potential for 120 s. Then repetitive

    Techniques Used: Blocking Assay

    35) Product Images from "Exploring the Structure of the Voltage-gated Na+ Channel by an Engineered Drug Access Pathway to the Receptor Site for Local Anesthetics *"

    Article Title: Exploring the Structure of the Voltage-gated Na+ Channel by an Engineered Drug Access Pathway to the Receptor Site for Local Anesthetics *

    Journal: The Journal of Biological Chemistry

    doi: 10.1074/jbc.M113.541763

    Structure of the external access pathway. The proposed molecular arrangement of crucial amino acids involved in access and binding of QX-222 is shown. A and B ), respectively, based
    Figure Legend Snippet: Structure of the external access pathway. The proposed molecular arrangement of crucial amino acids involved in access and binding of QX-222 is shown. A and B ), respectively, based

    Techniques Used: Binding Assay

    Recovery from block by intracellular QX-222. A 5-s-long 10-Hz pulse train was applied for repetitive openings of the channels to bind QX-222 to the inner vestibule. After the last pulse in the train, the cell was repolarized to −140 mV for various
    Figure Legend Snippet: Recovery from block by intracellular QX-222. A 5-s-long 10-Hz pulse train was applied for repetitive openings of the channels to bind QX-222 to the inner vestibule. After the last pulse in the train, the cell was repolarized to −140 mV for various

    Techniques Used: Blocking Assay

    The binding site for external QX-222 is in the internal vestibule. Modulation of the EAP by an additional mutation in the selectivity filter and by mutations of Trp-1531 is shown. The stimulation protocol and depiction are the same as in B. A , residue
    Figure Legend Snippet: The binding site for external QX-222 is in the internal vestibule. Modulation of the EAP by an additional mutation in the selectivity filter and by mutations of Trp-1531 is shown. The stimulation protocol and depiction are the same as in B. A , residue

    Techniques Used: Binding Assay, Mutagenesis

    Mutations at Site 1575 Open an EAP for QX-222
    Figure Legend Snippet: Mutations at Site 1575 Open an EAP for QX-222

    Techniques Used:

    Effect of QX-222 on inactivation properties of channels carrying mutations at site 1531. A , in W1531A, 500 μ m QX-222 significantly shifted the steady-state inactivation curve to hyperpolarized potentials. V 1/2 was −74.6 ± 0.6 and
    Figure Legend Snippet: Effect of QX-222 on inactivation properties of channels carrying mutations at site 1531. A , in W1531A, 500 μ m QX-222 significantly shifted the steady-state inactivation curve to hyperpolarized potentials. V 1/2 was −74.6 ± 0.6 and

    Techniques Used:

    External block by QX-222 is favored by replacement of Ile-1575 with amino acids of small size or with hydrophilic properties. Sodium currents were evoked by depolarizing pulses at a frequency of 2 Hz (see “Experimental Procedures”). Connecting
    Figure Legend Snippet: External block by QX-222 is favored by replacement of Ile-1575 with amino acids of small size or with hydrophilic properties. Sodium currents were evoked by depolarizing pulses at a frequency of 2 Hz (see “Experimental Procedures”). Connecting

    Techniques Used: Blocking Assay

    Use-dependent block by external QX-222. A 2-Hz pulse train was applied for 30 s at a holding potential of −120 mV. Thereafter, external perfusion with QX-222 was started while cells were kept at the holding potential for 120 s. Then repetitive
    Figure Legend Snippet: Use-dependent block by external QX-222. A 2-Hz pulse train was applied for 30 s at a holding potential of −120 mV. Thereafter, external perfusion with QX-222 was started while cells were kept at the holding potential for 120 s. Then repetitive

    Techniques Used: Blocking Assay

    36) Product Images from "Exploring the Structure of the Voltage-gated Na+ Channel by an Engineered Drug Access Pathway to the Receptor Site for Local Anesthetics *"

    Article Title: Exploring the Structure of the Voltage-gated Na+ Channel by an Engineered Drug Access Pathway to the Receptor Site for Local Anesthetics *

    Journal: The Journal of Biological Chemistry

    doi: 10.1074/jbc.M113.541763

    Structure of the external access pathway. The proposed molecular arrangement of crucial amino acids involved in access and binding of QX-222 is shown. A and B ), respectively, based
    Figure Legend Snippet: Structure of the external access pathway. The proposed molecular arrangement of crucial amino acids involved in access and binding of QX-222 is shown. A and B ), respectively, based

    Techniques Used: Binding Assay

    Recovery from block by intracellular QX-222. A 5-s-long 10-Hz pulse train was applied for repetitive openings of the channels to bind QX-222 to the inner vestibule. After the last pulse in the train, the cell was repolarized to −140 mV for various
    Figure Legend Snippet: Recovery from block by intracellular QX-222. A 5-s-long 10-Hz pulse train was applied for repetitive openings of the channels to bind QX-222 to the inner vestibule. After the last pulse in the train, the cell was repolarized to −140 mV for various

    Techniques Used: Blocking Assay

    The binding site for external QX-222 is in the internal vestibule. Modulation of the EAP by an additional mutation in the selectivity filter and by mutations of Trp-1531 is shown. The stimulation protocol and depiction are the same as in B. A , residue
    Figure Legend Snippet: The binding site for external QX-222 is in the internal vestibule. Modulation of the EAP by an additional mutation in the selectivity filter and by mutations of Trp-1531 is shown. The stimulation protocol and depiction are the same as in B. A , residue

    Techniques Used: Binding Assay, Mutagenesis

    Mutations at Site 1575 Open an EAP for QX-222
    Figure Legend Snippet: Mutations at Site 1575 Open an EAP for QX-222

    Techniques Used:

    Effect of QX-222 on inactivation properties of channels carrying mutations at site 1531. A , in W1531A, 500 μ m QX-222 significantly shifted the steady-state inactivation curve to hyperpolarized potentials. V 1/2 was −74.6 ± 0.6 and
    Figure Legend Snippet: Effect of QX-222 on inactivation properties of channels carrying mutations at site 1531. A , in W1531A, 500 μ m QX-222 significantly shifted the steady-state inactivation curve to hyperpolarized potentials. V 1/2 was −74.6 ± 0.6 and

    Techniques Used:

    External block by QX-222 is favored by replacement of Ile-1575 with amino acids of small size or with hydrophilic properties. Sodium currents were evoked by depolarizing pulses at a frequency of 2 Hz (see “Experimental Procedures”). Connecting
    Figure Legend Snippet: External block by QX-222 is favored by replacement of Ile-1575 with amino acids of small size or with hydrophilic properties. Sodium currents were evoked by depolarizing pulses at a frequency of 2 Hz (see “Experimental Procedures”). Connecting

    Techniques Used: Blocking Assay

    Use-dependent block by external QX-222. A 2-Hz pulse train was applied for 30 s at a holding potential of −120 mV. Thereafter, external perfusion with QX-222 was started while cells were kept at the holding potential for 120 s. Then repetitive
    Figure Legend Snippet: Use-dependent block by external QX-222. A 2-Hz pulse train was applied for 30 s at a holding potential of −120 mV. Thereafter, external perfusion with QX-222 was started while cells were kept at the holding potential for 120 s. Then repetitive

    Techniques Used: Blocking Assay

    37) Product Images from "Exploring the Structure of the Voltage-gated Na+ Channel by an Engineered Drug Access Pathway to the Receptor Site for Local Anesthetics *"

    Article Title: Exploring the Structure of the Voltage-gated Na+ Channel by an Engineered Drug Access Pathway to the Receptor Site for Local Anesthetics *

    Journal: The Journal of Biological Chemistry

    doi: 10.1074/jbc.M113.541763

    Structure of the external access pathway. The proposed molecular arrangement of crucial amino acids involved in access and binding of QX-222 is shown. A and B ), respectively, based
    Figure Legend Snippet: Structure of the external access pathway. The proposed molecular arrangement of crucial amino acids involved in access and binding of QX-222 is shown. A and B ), respectively, based

    Techniques Used: Binding Assay

    Recovery from block by intracellular QX-222. A 5-s-long 10-Hz pulse train was applied for repetitive openings of the channels to bind QX-222 to the inner vestibule. After the last pulse in the train, the cell was repolarized to −140 mV for various
    Figure Legend Snippet: Recovery from block by intracellular QX-222. A 5-s-long 10-Hz pulse train was applied for repetitive openings of the channels to bind QX-222 to the inner vestibule. After the last pulse in the train, the cell was repolarized to −140 mV for various

    Techniques Used: Blocking Assay

    The binding site for external QX-222 is in the internal vestibule. Modulation of the EAP by an additional mutation in the selectivity filter and by mutations of Trp-1531 is shown. The stimulation protocol and depiction are the same as in B. A , residue
    Figure Legend Snippet: The binding site for external QX-222 is in the internal vestibule. Modulation of the EAP by an additional mutation in the selectivity filter and by mutations of Trp-1531 is shown. The stimulation protocol and depiction are the same as in B. A , residue

    Techniques Used: Binding Assay, Mutagenesis

    Mutations at Site 1575 Open an EAP for QX-222
    Figure Legend Snippet: Mutations at Site 1575 Open an EAP for QX-222

    Techniques Used:

    Effect of QX-222 on inactivation properties of channels carrying mutations at site 1531. A , in W1531A, 500 μ m QX-222 significantly shifted the steady-state inactivation curve to hyperpolarized potentials. V 1/2 was −74.6 ± 0.6 and
    Figure Legend Snippet: Effect of QX-222 on inactivation properties of channels carrying mutations at site 1531. A , in W1531A, 500 μ m QX-222 significantly shifted the steady-state inactivation curve to hyperpolarized potentials. V 1/2 was −74.6 ± 0.6 and

    Techniques Used:

    External block by QX-222 is favored by replacement of Ile-1575 with amino acids of small size or with hydrophilic properties. Sodium currents were evoked by depolarizing pulses at a frequency of 2 Hz (see “Experimental Procedures”). Connecting
    Figure Legend Snippet: External block by QX-222 is favored by replacement of Ile-1575 with amino acids of small size or with hydrophilic properties. Sodium currents were evoked by depolarizing pulses at a frequency of 2 Hz (see “Experimental Procedures”). Connecting

    Techniques Used: Blocking Assay

    Use-dependent block by external QX-222. A 2-Hz pulse train was applied for 30 s at a holding potential of −120 mV. Thereafter, external perfusion with QX-222 was started while cells were kept at the holding potential for 120 s. Then repetitive
    Figure Legend Snippet: Use-dependent block by external QX-222. A 2-Hz pulse train was applied for 30 s at a holding potential of −120 mV. Thereafter, external perfusion with QX-222 was started while cells were kept at the holding potential for 120 s. Then repetitive

    Techniques Used: Blocking Assay

    38) Product Images from "Exploring the Structure of the Voltage-gated Na+ Channel by an Engineered Drug Access Pathway to the Receptor Site for Local Anesthetics *"

    Article Title: Exploring the Structure of the Voltage-gated Na+ Channel by an Engineered Drug Access Pathway to the Receptor Site for Local Anesthetics *

    Journal: The Journal of Biological Chemistry

    doi: 10.1074/jbc.M113.541763

    Structure of the external access pathway. The proposed molecular arrangement of crucial amino acids involved in access and binding of QX-222 is shown. A and B ), respectively, based
    Figure Legend Snippet: Structure of the external access pathway. The proposed molecular arrangement of crucial amino acids involved in access and binding of QX-222 is shown. A and B ), respectively, based

    Techniques Used: Binding Assay

    Recovery from block by intracellular QX-222. A 5-s-long 10-Hz pulse train was applied for repetitive openings of the channels to bind QX-222 to the inner vestibule. After the last pulse in the train, the cell was repolarized to −140 mV for various
    Figure Legend Snippet: Recovery from block by intracellular QX-222. A 5-s-long 10-Hz pulse train was applied for repetitive openings of the channels to bind QX-222 to the inner vestibule. After the last pulse in the train, the cell was repolarized to −140 mV for various

    Techniques Used: Blocking Assay

    The binding site for external QX-222 is in the internal vestibule. Modulation of the EAP by an additional mutation in the selectivity filter and by mutations of Trp-1531 is shown. The stimulation protocol and depiction are the same as in B. A , residue
    Figure Legend Snippet: The binding site for external QX-222 is in the internal vestibule. Modulation of the EAP by an additional mutation in the selectivity filter and by mutations of Trp-1531 is shown. The stimulation protocol and depiction are the same as in B. A , residue

    Techniques Used: Binding Assay, Mutagenesis

    Mutations at Site 1575 Open an EAP for QX-222
    Figure Legend Snippet: Mutations at Site 1575 Open an EAP for QX-222

    Techniques Used:

    Effect of QX-222 on inactivation properties of channels carrying mutations at site 1531. A , in W1531A, 500 μ m QX-222 significantly shifted the steady-state inactivation curve to hyperpolarized potentials. V 1/2 was −74.6 ± 0.6 and
    Figure Legend Snippet: Effect of QX-222 on inactivation properties of channels carrying mutations at site 1531. A , in W1531A, 500 μ m QX-222 significantly shifted the steady-state inactivation curve to hyperpolarized potentials. V 1/2 was −74.6 ± 0.6 and

    Techniques Used:

    External block by QX-222 is favored by replacement of Ile-1575 with amino acids of small size or with hydrophilic properties. Sodium currents were evoked by depolarizing pulses at a frequency of 2 Hz (see “Experimental Procedures”). Connecting
    Figure Legend Snippet: External block by QX-222 is favored by replacement of Ile-1575 with amino acids of small size or with hydrophilic properties. Sodium currents were evoked by depolarizing pulses at a frequency of 2 Hz (see “Experimental Procedures”). Connecting

    Techniques Used: Blocking Assay

    Use-dependent block by external QX-222. A 2-Hz pulse train was applied for 30 s at a holding potential of −120 mV. Thereafter, external perfusion with QX-222 was started while cells were kept at the holding potential for 120 s. Then repetitive
    Figure Legend Snippet: Use-dependent block by external QX-222. A 2-Hz pulse train was applied for 30 s at a holding potential of −120 mV. Thereafter, external perfusion with QX-222 was started while cells were kept at the holding potential for 120 s. Then repetitive

    Techniques Used: Blocking Assay

    39) Product Images from "Exploring the Structure of the Voltage-gated Na+ Channel by an Engineered Drug Access Pathway to the Receptor Site for Local Anesthetics *"

    Article Title: Exploring the Structure of the Voltage-gated Na+ Channel by an Engineered Drug Access Pathway to the Receptor Site for Local Anesthetics *

    Journal: The Journal of Biological Chemistry

    doi: 10.1074/jbc.M113.541763

    Structure of the external access pathway. The proposed molecular arrangement of crucial amino acids involved in access and binding of QX-222 is shown. A and B ), respectively, based
    Figure Legend Snippet: Structure of the external access pathway. The proposed molecular arrangement of crucial amino acids involved in access and binding of QX-222 is shown. A and B ), respectively, based

    Techniques Used: Binding Assay

    Recovery from block by intracellular QX-222. A 5-s-long 10-Hz pulse train was applied for repetitive openings of the channels to bind QX-222 to the inner vestibule. After the last pulse in the train, the cell was repolarized to −140 mV for various
    Figure Legend Snippet: Recovery from block by intracellular QX-222. A 5-s-long 10-Hz pulse train was applied for repetitive openings of the channels to bind QX-222 to the inner vestibule. After the last pulse in the train, the cell was repolarized to −140 mV for various

    Techniques Used: Blocking Assay

    The binding site for external QX-222 is in the internal vestibule. Modulation of the EAP by an additional mutation in the selectivity filter and by mutations of Trp-1531 is shown. The stimulation protocol and depiction are the same as in B. A , residue
    Figure Legend Snippet: The binding site for external QX-222 is in the internal vestibule. Modulation of the EAP by an additional mutation in the selectivity filter and by mutations of Trp-1531 is shown. The stimulation protocol and depiction are the same as in B. A , residue

    Techniques Used: Binding Assay, Mutagenesis

    Mutations at Site 1575 Open an EAP for QX-222
    Figure Legend Snippet: Mutations at Site 1575 Open an EAP for QX-222

    Techniques Used:

    Effect of QX-222 on inactivation properties of channels carrying mutations at site 1531. A , in W1531A, 500 μ m QX-222 significantly shifted the steady-state inactivation curve to hyperpolarized potentials. V 1/2 was −74.6 ± 0.6 and
    Figure Legend Snippet: Effect of QX-222 on inactivation properties of channels carrying mutations at site 1531. A , in W1531A, 500 μ m QX-222 significantly shifted the steady-state inactivation curve to hyperpolarized potentials. V 1/2 was −74.6 ± 0.6 and

    Techniques Used:

    External block by QX-222 is favored by replacement of Ile-1575 with amino acids of small size or with hydrophilic properties. Sodium currents were evoked by depolarizing pulses at a frequency of 2 Hz (see “Experimental Procedures”). Connecting
    Figure Legend Snippet: External block by QX-222 is favored by replacement of Ile-1575 with amino acids of small size or with hydrophilic properties. Sodium currents were evoked by depolarizing pulses at a frequency of 2 Hz (see “Experimental Procedures”). Connecting

    Techniques Used: Blocking Assay

    Use-dependent block by external QX-222. A 2-Hz pulse train was applied for 30 s at a holding potential of −120 mV. Thereafter, external perfusion with QX-222 was started while cells were kept at the holding potential for 120 s. Then repetitive
    Figure Legend Snippet: Use-dependent block by external QX-222. A 2-Hz pulse train was applied for 30 s at a holding potential of −120 mV. Thereafter, external perfusion with QX-222 was started while cells were kept at the holding potential for 120 s. Then repetitive

    Techniques Used: Blocking Assay

    40) Product Images from "Exploring the Structure of the Voltage-gated Na+ Channel by an Engineered Drug Access Pathway to the Receptor Site for Local Anesthetics *"

    Article Title: Exploring the Structure of the Voltage-gated Na+ Channel by an Engineered Drug Access Pathway to the Receptor Site for Local Anesthetics *

    Journal: The Journal of Biological Chemistry

    doi: 10.1074/jbc.M113.541763

    Structure of the external access pathway. The proposed molecular arrangement of crucial amino acids involved in access and binding of QX-222 is shown. A and B ), respectively, based
    Figure Legend Snippet: Structure of the external access pathway. The proposed molecular arrangement of crucial amino acids involved in access and binding of QX-222 is shown. A and B ), respectively, based

    Techniques Used: Binding Assay

    Recovery from block by intracellular QX-222. A 5-s-long 10-Hz pulse train was applied for repetitive openings of the channels to bind QX-222 to the inner vestibule. After the last pulse in the train, the cell was repolarized to −140 mV for various
    Figure Legend Snippet: Recovery from block by intracellular QX-222. A 5-s-long 10-Hz pulse train was applied for repetitive openings of the channels to bind QX-222 to the inner vestibule. After the last pulse in the train, the cell was repolarized to −140 mV for various

    Techniques Used: Blocking Assay

    The binding site for external QX-222 is in the internal vestibule. Modulation of the EAP by an additional mutation in the selectivity filter and by mutations of Trp-1531 is shown. The stimulation protocol and depiction are the same as in B. A , residue
    Figure Legend Snippet: The binding site for external QX-222 is in the internal vestibule. Modulation of the EAP by an additional mutation in the selectivity filter and by mutations of Trp-1531 is shown. The stimulation protocol and depiction are the same as in B. A , residue

    Techniques Used: Binding Assay, Mutagenesis

    Mutations at Site 1575 Open an EAP for QX-222
    Figure Legend Snippet: Mutations at Site 1575 Open an EAP for QX-222

    Techniques Used:

    Effect of QX-222 on inactivation properties of channels carrying mutations at site 1531. A , in W1531A, 500 μ m QX-222 significantly shifted the steady-state inactivation curve to hyperpolarized potentials. V 1/2 was −74.6 ± 0.6 and
    Figure Legend Snippet: Effect of QX-222 on inactivation properties of channels carrying mutations at site 1531. A , in W1531A, 500 μ m QX-222 significantly shifted the steady-state inactivation curve to hyperpolarized potentials. V 1/2 was −74.6 ± 0.6 and

    Techniques Used:

    External block by QX-222 is favored by replacement of Ile-1575 with amino acids of small size or with hydrophilic properties. Sodium currents were evoked by depolarizing pulses at a frequency of 2 Hz (see “Experimental Procedures”). Connecting
    Figure Legend Snippet: External block by QX-222 is favored by replacement of Ile-1575 with amino acids of small size or with hydrophilic properties. Sodium currents were evoked by depolarizing pulses at a frequency of 2 Hz (see “Experimental Procedures”). Connecting

    Techniques Used: Blocking Assay

    Use-dependent block by external QX-222. A 2-Hz pulse train was applied for 30 s at a holding potential of −120 mV. Thereafter, external perfusion with QX-222 was started while cells were kept at the holding potential for 120 s. Then repetitive
    Figure Legend Snippet: Use-dependent block by external QX-222. A 2-Hz pulse train was applied for 30 s at a holding potential of −120 mV. Thereafter, external perfusion with QX-222 was started while cells were kept at the holding potential for 120 s. Then repetitive

    Techniques Used: Blocking Assay

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    Alomone Labs qx 222
    Structure of the external access pathway. The proposed molecular arrangement of crucial amino acids involved in access and binding of <t>QX-222</t> is shown. A and B ), respectively, based
    Qx 222, supplied by Alomone Labs, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Structure of the external access pathway. The proposed molecular arrangement of crucial amino acids involved in access and binding of QX-222 is shown. A and B ), respectively, based

    Journal: The Journal of Biological Chemistry

    Article Title: Exploring the Structure of the Voltage-gated Na+ Channel by an Engineered Drug Access Pathway to the Receptor Site for Local Anesthetics *

    doi: 10.1074/jbc.M113.541763

    Figure Lengend Snippet: Structure of the external access pathway. The proposed molecular arrangement of crucial amino acids involved in access and binding of QX-222 is shown. A and B ), respectively, based

    Article Snippet: To explore this possibility, we held the channels at a potential of −120 mV while applying QX-222 externally for 120 s. During this period, channels are expected to reside in the closed state.

    Techniques: Binding Assay

    Recovery from block by intracellular QX-222. A 5-s-long 10-Hz pulse train was applied for repetitive openings of the channels to bind QX-222 to the inner vestibule. After the last pulse in the train, the cell was repolarized to −140 mV for various

    Journal: The Journal of Biological Chemistry

    Article Title: Exploring the Structure of the Voltage-gated Na+ Channel by an Engineered Drug Access Pathway to the Receptor Site for Local Anesthetics *

    doi: 10.1074/jbc.M113.541763

    Figure Lengend Snippet: Recovery from block by intracellular QX-222. A 5-s-long 10-Hz pulse train was applied for repetitive openings of the channels to bind QX-222 to the inner vestibule. After the last pulse in the train, the cell was repolarized to −140 mV for various

    Article Snippet: To explore this possibility, we held the channels at a potential of −120 mV while applying QX-222 externally for 120 s. During this period, channels are expected to reside in the closed state.

    Techniques: Blocking Assay

    The binding site for external QX-222 is in the internal vestibule. Modulation of the EAP by an additional mutation in the selectivity filter and by mutations of Trp-1531 is shown. The stimulation protocol and depiction are the same as in B. A , residue

    Journal: The Journal of Biological Chemistry

    Article Title: Exploring the Structure of the Voltage-gated Na+ Channel by an Engineered Drug Access Pathway to the Receptor Site for Local Anesthetics *

    doi: 10.1074/jbc.M113.541763

    Figure Lengend Snippet: The binding site for external QX-222 is in the internal vestibule. Modulation of the EAP by an additional mutation in the selectivity filter and by mutations of Trp-1531 is shown. The stimulation protocol and depiction are the same as in B. A , residue

    Article Snippet: To explore this possibility, we held the channels at a potential of −120 mV while applying QX-222 externally for 120 s. During this period, channels are expected to reside in the closed state.

    Techniques: Binding Assay, Mutagenesis

    Mutations at Site 1575 Open an EAP for QX-222

    Journal: The Journal of Biological Chemistry

    Article Title: Exploring the Structure of the Voltage-gated Na+ Channel by an Engineered Drug Access Pathway to the Receptor Site for Local Anesthetics *

    doi: 10.1074/jbc.M113.541763

    Figure Lengend Snippet: Mutations at Site 1575 Open an EAP for QX-222

    Article Snippet: To explore this possibility, we held the channels at a potential of −120 mV while applying QX-222 externally for 120 s. During this period, channels are expected to reside in the closed state.

    Techniques:

    Effect of QX-222 on inactivation properties of channels carrying mutations at site 1531. A , in W1531A, 500 μ m QX-222 significantly shifted the steady-state inactivation curve to hyperpolarized potentials. V 1/2 was −74.6 ± 0.6 and

    Journal: The Journal of Biological Chemistry

    Article Title: Exploring the Structure of the Voltage-gated Na+ Channel by an Engineered Drug Access Pathway to the Receptor Site for Local Anesthetics *

    doi: 10.1074/jbc.M113.541763

    Figure Lengend Snippet: Effect of QX-222 on inactivation properties of channels carrying mutations at site 1531. A , in W1531A, 500 μ m QX-222 significantly shifted the steady-state inactivation curve to hyperpolarized potentials. V 1/2 was −74.6 ± 0.6 and

    Article Snippet: To explore this possibility, we held the channels at a potential of −120 mV while applying QX-222 externally for 120 s. During this period, channels are expected to reside in the closed state.

    Techniques:

    External block by QX-222 is favored by replacement of Ile-1575 with amino acids of small size or with hydrophilic properties. Sodium currents were evoked by depolarizing pulses at a frequency of 2 Hz (see “Experimental Procedures”). Connecting

    Journal: The Journal of Biological Chemistry

    Article Title: Exploring the Structure of the Voltage-gated Na+ Channel by an Engineered Drug Access Pathway to the Receptor Site for Local Anesthetics *

    doi: 10.1074/jbc.M113.541763

    Figure Lengend Snippet: External block by QX-222 is favored by replacement of Ile-1575 with amino acids of small size or with hydrophilic properties. Sodium currents were evoked by depolarizing pulses at a frequency of 2 Hz (see “Experimental Procedures”). Connecting

    Article Snippet: To explore this possibility, we held the channels at a potential of −120 mV while applying QX-222 externally for 120 s. During this period, channels are expected to reside in the closed state.

    Techniques: Blocking Assay

    Use-dependent block by external QX-222. A 2-Hz pulse train was applied for 30 s at a holding potential of −120 mV. Thereafter, external perfusion with QX-222 was started while cells were kept at the holding potential for 120 s. Then repetitive

    Journal: The Journal of Biological Chemistry

    Article Title: Exploring the Structure of the Voltage-gated Na+ Channel by an Engineered Drug Access Pathway to the Receptor Site for Local Anesthetics *

    doi: 10.1074/jbc.M113.541763

    Figure Lengend Snippet: Use-dependent block by external QX-222. A 2-Hz pulse train was applied for 30 s at a holding potential of −120 mV. Thereafter, external perfusion with QX-222 was started while cells were kept at the holding potential for 120 s. Then repetitive

    Article Snippet: To explore this possibility, we held the channels at a potential of −120 mV while applying QX-222 externally for 120 s. During this period, channels are expected to reside in the closed state.

    Techniques: Blocking Assay