Animal toxins can alter the function of Nav1.8 and Nav1.9. - Wikidata - awgldk - TriplyDB

Animal toxins can alter the function of Nav1.8 and Nav1.9.

Animal toxins can alter the function of Nav1.8 and Nav1.9.

http://www.wikidata.org/entity/Q36246739

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The hitchhiker's guide to the voltage-gated sodium channel galaxy Voltage-gated sodium channel in grasshopper mice defends against bark scorpion toxin Conotoxins targeting neuronal voltage-gated sodium channel subtypes: potential analgesics?Effect of amitriptyline on tetrodotoxin-resistant Nav1.9 currents in nociceptive trigeminal neurons.Pathological nociceptors in two patients with erythromelalgia-like symptoms and rare genetic Nav 1.9 variants Animal toxins influence voltage-gated sodium channel function.Venom-based biotoxins as potential analgesics.Venom: the sharp end of pain therapeutics Dependence of Nociceptive Detection Thresholds on Physiological Parameters and Capsaicin-Induced Neuroplasticity: A Computational Study Physiological and biochemical analysis to reveal the molecular basis for black widow spiderling toxicity.Reduced excitability of gp130-deficient nociceptors is associated with increased voltage-gated potassium currents and Kcna4 channel upregulation.

P2860

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P2860

Animal toxins can alter the function of Nav1.8 and Nav1.9.

http://www.wikidata.org/entity/Q36246739

description

2012 nî lūn-bûn

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2012年の論文

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2012年論文

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2012年論文

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2012年論文

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2012年論文

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2012年論文

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2012年论文

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2012年论文

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2012年论文

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name

Animal toxins can alter the function of Nav1.8 and Nav1.9.

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Animal toxins can alter the function of Nav1.8 and Nav1.9.

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type

label

Animal toxins can alter the function of Nav1.8 and Nav1.9.

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Animal toxins can alter the function of Nav1.8 and Nav1.9.

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prefLabel

Animal toxins can alter the function of Nav1.8 and Nav1.9.

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Animal toxins can alter the function of Nav1.8 and Nav1.9.

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Animal toxins can alter the function of Nav1.8 and Nav1.9.

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Frank Bosmans

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John Gilchrist

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Creative Commons Attribution 3.0 Unported

P2860

X-ray structure of a voltage-dependent K+ channel

Improved patch-clamp techniques for high-resolution current recording from cells and cell-free membrane patches

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

Portability of paddle motif function and pharmacology in voltage sensors

Interactions between lipids and voltage sensor paddles detected with tarantula toxins

Tarantula toxins interact with voltage sensors within lipid membranes

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

Neurotrophin-evoked depolarization requires the sodium channel Na(V)1.9

NaN/Nav1.9: a sodium channel with unique properties

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

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8

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23012651

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transport protein

membrane proteins

nerve tissue proteins

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3446747

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