qx 222 Search Results


  • Logo
  • About
  • News
  • Press Release
  • Team
  • Advisors
  • Partners
  • Contact
  • Bioz Stars
  • Bioz vStars
  • 86
    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
    Average 86 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    qx 222 - by Bioz Stars, 2022-08
    86/100 stars
      Buy from Supplier

    85
    Tocris qx 222 cl
    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 Cl, supplied by Tocris, used in various techniques. Bioz Stars score: 85/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/qx 222 cl/product/Tocris
    Average 85 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    qx 222 cl - by Bioz Stars, 2022-08
    85/100 stars
      Buy from Supplier

    86
    Tocris n trimethyl 2 oxoethaniminium chloride
    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
    N Trimethyl 2 Oxoethaniminium Chloride, supplied by Tocris, 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/n trimethyl 2 oxoethaniminium chloride/product/Tocris
    Average 86 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    n trimethyl 2 oxoethaniminium chloride - by Bioz Stars, 2022-08
    86/100 stars
      Buy from Supplier

    Image Search Results


    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: Hence QX-222 may act as an allosteric modulator of inactivation, a concept that has been proposed previously as a mechanism for local anesthetic drug action ( ).

    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: Hence QX-222 may act as an allosteric modulator of inactivation, a concept that has been proposed previously as a mechanism for local anesthetic drug action ( ).

    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: Hence QX-222 may act as an allosteric modulator of inactivation, a concept that has been proposed previously as a mechanism for local anesthetic drug action ( ).

    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: Hence QX-222 may act as an allosteric modulator of inactivation, a concept that has been proposed previously as a mechanism for local anesthetic drug action ( ).

    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: Hence QX-222 may act as an allosteric modulator of inactivation, a concept that has been proposed previously as a mechanism for local anesthetic drug action ( ).

    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: Hence QX-222 may act as an allosteric modulator of inactivation, a concept that has been proposed previously as a mechanism for local anesthetic drug action ( ).

    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: Hence QX-222 may act as an allosteric modulator of inactivation, a concept that has been proposed previously as a mechanism for local anesthetic drug action ( ).

    Techniques: Blocking Assay