qx 222 (Alomone Labs)
Alomone Labs is a verified supplier 
Alomone Labs manufactures this product 
86
Structured Review
Alomone Labs
qx 222
Qx 222, supplied by Alomone Labs, used in various techniques. Bioz Stars score: 86/100, based on 40 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/result/qx 222/product/Alomone Labs
Average 86 stars, based on 40 article reviews
Price from $9.99 to $1999.99
Qx 222, supplied by Alomone Labs, used in various techniques. Bioz Stars score: 86/100, based on 40 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/result/qx 222/product/Alomone Labs
Average 86 stars, based on 40 article reviews
Price from $9.99 to $1999.99
qx 222 - by Bioz Stars,
2022-08
86/100 stars
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
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
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
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
Figure Legend Snippet: Mutations at Site 1575 Open an EAP for QX-222
Techniques Used:
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:
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
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
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
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
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
Figure Legend Snippet: Mutations at Site 1575 Open an EAP for QX-222
Techniques Used:
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:
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
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
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
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
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
Figure Legend Snippet: Mutations at Site 1575 Open an EAP for QX-222
Techniques Used:
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:
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
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
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
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
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
Figure Legend Snippet: Mutations at Site 1575 Open an EAP for QX-222
Techniques Used:
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:
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
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
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
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
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
Figure Legend Snippet: Mutations at Site 1575 Open an EAP for QX-222
Techniques Used:
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:
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
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
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
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
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
Figure Legend Snippet: Mutations at Site 1575 Open an EAP for QX-222
Techniques Used:
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:
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
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
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
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
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
Figure Legend Snippet: Mutations at Site 1575 Open an EAP for QX-222
Techniques Used:
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:
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
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
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
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
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
Figure Legend Snippet: Mutations at Site 1575 Open an EAP for QX-222
Techniques Used:
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:
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
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
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
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
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
Figure Legend Snippet: Mutations at Site 1575 Open an EAP for QX-222
Techniques Used:
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:
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
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
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
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
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
Figure Legend Snippet: Mutations at Site 1575 Open an EAP for QX-222
Techniques Used:
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:
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
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
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
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
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
Figure Legend Snippet: Mutations at Site 1575 Open an EAP for QX-222
Techniques Used:
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:
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
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
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
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
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
Figure Legend Snippet: Mutations at Site 1575 Open an EAP for QX-222
Techniques Used:
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:
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
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
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
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
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
Figure Legend Snippet: Mutations at Site 1575 Open an EAP for QX-222
Techniques Used:
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:
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
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
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
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
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
Figure Legend Snippet: Mutations at Site 1575 Open an EAP for QX-222
Techniques Used:
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:
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
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
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
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
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
Figure Legend Snippet: Mutations at Site 1575 Open an EAP for QX-222
Techniques Used:
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:
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
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
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
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
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
Figure Legend Snippet: Mutations at Site 1575 Open an EAP for QX-222
Techniques Used:
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:
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
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
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
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
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
Figure Legend Snippet: Mutations at Site 1575 Open an EAP for QX-222
Techniques Used:
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:
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
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
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
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
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
Figure Legend Snippet: Mutations at Site 1575 Open an EAP for QX-222
Techniques Used:
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:
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
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
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
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
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
Figure Legend Snippet: Mutations at Site 1575 Open an EAP for QX-222
Techniques Used:
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:
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
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
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
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
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
Figure Legend Snippet: Mutations at Site 1575 Open an EAP for QX-222
Techniques Used:
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:
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
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
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
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
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
Figure Legend Snippet: Mutations at Site 1575 Open an EAP for QX-222
Techniques Used:
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:
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
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
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
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
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
Figure Legend Snippet: Mutations at Site 1575 Open an EAP for QX-222
Techniques Used:
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:
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
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
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
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
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
Figure Legend Snippet: Mutations at Site 1575 Open an EAP for QX-222
Techniques Used:
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:
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
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
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
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
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
Figure Legend Snippet: Mutations at Site 1575 Open an EAP for QX-222
Techniques Used:
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:
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
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
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
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
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
Figure Legend Snippet: Mutations at Site 1575 Open an EAP for QX-222
Techniques Used:
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:
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
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
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
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
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
Figure Legend Snippet: Mutations at Site 1575 Open an EAP for QX-222
Techniques Used:
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:
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
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
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
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
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
Figure Legend Snippet: Mutations at Site 1575 Open an EAP for QX-222
Techniques Used:
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:
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
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
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
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
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
Figure Legend Snippet: Mutations at Site 1575 Open an EAP for QX-222
Techniques Used:
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:
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
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
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
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
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
Figure Legend Snippet: Mutations at Site 1575 Open an EAP for QX-222
Techniques Used:
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:
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
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
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
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
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
Figure Legend Snippet: Mutations at Site 1575 Open an EAP for QX-222
Techniques Used:
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:
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
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
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
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
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
Figure Legend Snippet: Mutations at Site 1575 Open an EAP for QX-222
Techniques Used:
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:
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
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
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
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
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
Figure Legend Snippet: Mutations at Site 1575 Open an EAP for QX-222
Techniques Used:
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:
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
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
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
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
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
Figure Legend Snippet: Mutations at Site 1575 Open an EAP for QX-222
Techniques Used:
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:
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
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
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
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
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
Figure Legend Snippet: Mutations at Site 1575 Open an EAP for QX-222
Techniques Used:
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:
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
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
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
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
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
Figure Legend Snippet: Mutations at Site 1575 Open an EAP for QX-222
Techniques Used:
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:
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
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
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
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
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
Figure Legend Snippet: Mutations at Site 1575 Open an EAP for QX-222
Techniques Used:
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:
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
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
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
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
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
Figure Legend Snippet: Mutations at Site 1575 Open an EAP for QX-222
Techniques Used:
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:
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
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
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
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
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
Figure Legend Snippet: Mutations at Site 1575 Open an EAP for QX-222
Techniques Used:
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:
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
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
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
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
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
Figure Legend Snippet: Mutations at Site 1575 Open an EAP for QX-222
Techniques Used:
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:
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
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
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
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
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
Figure Legend Snippet: Mutations at Site 1575 Open an EAP for QX-222
Techniques Used:
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:
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
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