Mapping the receptor site for alpha-scorpion toxins on a Na+ channel voltage sensor - sprookjes - yvandenbroek - TriplyDB

Mapping the receptor site for alpha-scorpion toxins on a Na+ channel voltage sensor

Mapping the receptor site for alpha-scorpion toxins on a Na+ channel voltage sensor

http://www.wikidata.org/entity/Q24635953

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Biotechnological Trends in Spider and Scorpion Antivenom Development The hitchhiker's guide to the voltage-gated sodium channel galaxy Computational Studies of Venom Peptides Targeting Potassium Channels From foe to friend: using animal toxins to investigate ion channel function Crystal structure of a voltage-gated sodium channel in two potentially inactivated states Proton-dependent inhibition of the cardiac sodium channel Nav1.5 by ranolazine Selective spider toxins reveal a role for the Nav1.1 channel in mechanical pain Structure and function of voltage-gated sodium channels at atomic resolution.Modular organization of α-toxins from scorpion venom mirrors domain structure of their targets, sodium channels.Synergetic action of domain II and IV underlies persistent current generation in Nav1.3 as revealed by a tarantula toxin.Scorpion venom components that affect ion-channels function Molecular determinants of Hv1 proton channel inhibition by guanidine derivatives.Three charged amino acids in extracellular loop 1 are involved in maintaining the outer pore architecture of CFTR.Synthesis and analgesic effects of μ-TRTX-Hhn1b on models of inflammatory and neuropathic pain.Voltage-gated sodium channels at 60: structure, function and pathophysiology.Paxilline inhibits BK channels by an almost exclusively closed-channel block mechanism.Bacterial voltage-gated sodium channels (BacNa(V)s) from the soil, sea, and salt lakes enlighten molecular mechanisms of electrical signaling and pharmacology in the brain and heart.A surface plasmon resonance approach to monitor toxin interactions with an isolated voltage-gated sodium channel paddle motif.Direct evidence that scorpion α-toxins (site-3) modulate sodium channel inactivation by hindrance of voltage-sensor movements The Scorpion Toxin Tf2 from Tityus fasciolatus Promotes Nav1.3 Opening.Binding modes of μ-conotoxin to the bacterial sodium channel (NaVAb)Sequence variations at I260 and A1731 contribute to persistent currents in Drosophila sodium channels.Computer Simulations of Voltage-Gated Cation Channels Target-Driven Evolution of Scorpion Toxins Allosteric interactions between receptor site 3 and 4 of voltage-gated sodium channels: a novel perspective for the underlying mechanism of scorpion sting-induced pain.Mapping the interaction site for a β-scorpion toxin in the pore module of domain III of voltage-gated Na(+) channels Structural Insights into the Atomistic Mechanisms of Action of Small Molecule Inhibitors Targeting the KCa3.1 Channel Pore.Finding Channels.Opening the shaker K+ channel with hanatoxin.Structure and function of hainantoxin-III, a selective antagonist of neuronal tetrodotoxin-sensitive voltage-gated sodium channels isolated from the Chinese bird spider Ornithoctonus hainana.Voltage sensor interaction site for selective small molecule inhibitors of voltage-gated sodium channels.Modulation of human Nav1.7 channel gating by synthetic α-scorpion toxin OD1 and its analogs.Computational methods of studying the binding of toxins from venomous animals to biological ion channels: theory and applications.Fluorescent protein-scorpion toxin chimera is a convenient molecular tool for studies of potassium channels Shellfish toxins targeting voltage-gated sodium channels.Characterization of a novel BmαTX47 toxin modulating sodium channels: the crucial role of expression vectors in toxin pharmacological activity.The insecticidal potential of venom peptides.Animal toxins influence voltage-gated sodium channel function.Molecular Simulations of Disulfide-Rich Venom Peptides with Ion Channels and Membranes.The Molecular Basis of Toxins' Interactions with Intracellular Signaling via Discrete Portals.

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P2860

Mapping the receptor site for alpha-scorpion toxins on a Na+ channel voltage sensor

http://www.wikidata.org/entity/Q24635953

description

2011 nî lūn-bûn

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2011 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած

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Mapping the receptor site for alpha-scorpion toxins on a Na+ channel voltage sensor

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Mapping the receptor site for alpha-scorpion toxins on a Na+ channel voltage sensor

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Mapping the receptor site for alpha-scorpion toxins on a Na+ channel voltage sensor

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Mapping the receptor site for alpha-scorpion toxins on a Na+ channel voltage sensor

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Mapping the receptor site for alpha-scorpion toxins on a Na+ channel voltage sensor

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Mapping the receptor site for alpha-scorpion toxins on a Na+ channel voltage sensor

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Mapping the receptor site for alpha-scorpion toxins on a Na+ channel voltage sensor

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Mapping the receptor site for alpha-scorpion toxins on a Na+ channel voltage sensor

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Mapping the receptor site for alpha-scorpion toxins on a Na+ channel voltage sensor

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

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Mapping the receptor site for alpha-scorpion toxins on a Na+ channel voltage sensor

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Dalia Gordon

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Jinti Wang

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Michael Gurevitz

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Roy Kahn

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Todd Scheuer

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Vladimir Yarov-Yarovoy

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William A Catterall

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P2860

A quantitative description of membrane current and its application to conduction and excitation in nerve

Crystal structure and mechanism of a calcium-gated potassium channel

Atomic structure of a voltage-dependent K+ channel in a lipid membrane-like environment

Crystal structure of toxin II from the scorpion Androctonus australis Hector refined at 1.3 A resolution

UCSF Chimera--a visualization system for exploratory research and analysis

From ionic currents to molecular mechanisms: the structure and function of voltage-gated sodium channels

Protein-protein docking with simultaneous optimization of rigid-body displacement and side-chain conformations

Crystal structure of a mammalian voltage-dependent Shaker family K+ channel

Multiple sequence alignment with Clustal X

Protein structure prediction using Rosetta

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37

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21876146

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