A disulfide tether stabilizes the block of sodium channels by the conotoxin μO§-GVIIJ. - sprookjes - yvandenbroek - TriplyDB

A disulfide tether stabilizes the block of sodium channels by the conotoxin μO§-GVIIJ.

A disulfide tether stabilizes the block of sodium channels by the conotoxin μO§-GVIIJ.

http://www.wikidata.org/entity/Q37599922

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The hitchhiker's guide to the voltage-gated sodium channel galaxy Conotoxins That Could Provide Analgesia through Voltage Gated Sodium Channel Inhibition Structure and function of μ-conotoxins, peptide-based sodium channel blockers with analgesic activity Evaluation of recombinant monoclonal antibody SVmab1 binding to Na V1.7 target sequences and block of human Na V1.7 currents Insights into the origins of fish hunting in venomous cone snails from studies of Conus tessulatus Conotoxin gene superfamilies.Α- and β-subunit composition of voltage-gated sodium channels investigated with μ-conotoxins and the recently discovered μO§-conotoxin GVIIJ.Optimized deep-targeted proteotranscriptomic profiling reveals unexplored Conus toxin diversity and novel cysteine frameworks.Binary architecture of the Nav1.2-β2 signaling complex Structural Basis for the Inhibition of Voltage-gated Sodium Channels by Conotoxin μO§-GVIIJ.Therapeutic conotoxins: a US patent literature survey.µ-Conotoxins Modulating Sodium Currents in Pain Perception and Transmission: A Therapeutic Potential.Voltage-gated sodium channel β subunits: The power outside the pore in brain development and disease.Venom peptides as therapeutics: advances, challenges and the future of venom-peptide discovery.Generation of therapeutic immunoconjugates via Residue-Specific Conjugation Technology (RESPECT) utilizing a native cysteine in the light chain framework of Oryctolagus cuniculus.

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A disulfide tether stabilizes the block of sodium channels by the conotoxin μO§-GVIIJ.

http://www.wikidata.org/entity/Q37599922

description

article científic

@ca

article scientifique

@fr

articolo scientifico

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artigo científico

@pt

bilimsel makale

@tr

scientific article published on 04 February 2014

@en

vedecký článok

@sk

vetenskaplig artikel

@sv

videnskabelig artikel

@da

vědecký článek

@cs

name

A disulfide tether stabilizes the block of sodium channels by the conotoxin μO§-GVIIJ.

@en

A disulfide tether stabilizes the block of sodium channels by the conotoxin μO§-GVIIJ.

@nl

type

label

A disulfide tether stabilizes the block of sodium channels by the conotoxin μO§-GVIIJ.

@en

A disulfide tether stabilizes the block of sodium channels by the conotoxin μO§-GVIIJ.

@nl

prefLabel

A disulfide tether stabilizes the block of sodium channels by the conotoxin μO§-GVIIJ.

@en

A disulfide tether stabilizes the block of sodium channels by the conotoxin μO§-GVIIJ.

@nl

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PNAS.1324189111

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Proceedings of the National Academy of Sciences of the United States of America

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A disulfide tether stabilizes the block of sodium channels by the conotoxin μO§-GVIIJ.

@en

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Alan D Wickenden

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Baldomero M Olivera

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Brad R Green

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Doju Yoshikami

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Grzegorz Bulaj

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H Mimi Zhou

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Joanna Gajewiak

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Julita Imperial

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Layla Azam

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Mack Flinspach

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P2860

Cooccupancy of the outer vestibule of voltage-gated sodium channels by micro-conotoxin KIIIA and saxitoxin or tetrodotoxin

Conus venom peptide pharmacology

International Union of Pharmacology. XLVII. Nomenclature and structure-function relationships of voltage-gated sodium channels

Control of transient, resurgent, and persistent current by open-channel block by Na channel beta4 in cultured cerebellar granule neurons

Gating properties of Na(v)1.7 and Na(v)1.8 peripheral nerve sodium channels.

Synergistic and antagonistic interactions between tetrodotoxin and mu-conotoxin in blocking voltage-gated sodium channels.

Molecular motions within the pore of voltage-dependent sodium channels

Molecular mechanisms of neurotoxin action on voltage-gated sodium channels.

Conus venoms: a rich source of novel ion channel-targeted peptides.

Extrapore residues of the S5-S6 loop of domain 2 of the voltage-gated skeletal muscle sodium channel (rSkM1) contribute to the mu-conotoxin GIIIA binding site.

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2758-2763

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scholarly article

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10.1073/PNAS.1324189111

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7

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111

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Beatrix Ueberheide

Aleksandra Walewska

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2014-02-04T00:00:00Z

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260108421

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