Direct regulation of prokaryotic Kir channel by cholesterol. - Wikidata - awgldk - TriplyDB

Direct regulation of prokaryotic Kir channel by cholesterol.

Direct regulation of prokaryotic Kir channel by cholesterol.

http://www.wikidata.org/entity/Q37431875

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Counterion-mediated pattern formation in membranes containing anionic lipids Mechanism for selectivity-inactivation coupling in KcsA potassium channels Structure of a KirBac potassium channel with an open bundle crossing indicates a mechanism of channel gating Using Sterol Substitution to Probe the Role of Membrane Domains in Membrane Functions.Cholesterol binding to ion channels Lipid-binding surfaces of membrane proteins: evidence from evolutionary and structural analysis Differential lipid dependence of the function of bacterial sodium channels Functional complementation and genetic deletion studies of KirBac channels: activatory mutations highlight gating-sensitive domains Enantioselective protein-sterol interactions mediate regulation of both prokaryotic and eukaryotic inward rectifier K+ channels by cholesterol.Cholesterol sensitivity of KIR2.1 is controlled by a belt of residues around the cytosolic pore.Acute cholesterol-induced anti-natriuretic effects: role of epithelial Na+ channel activity, protein levels, and processing.Interplay Between Lipid Modulators of Kir2 Channels: Cholesterol and PIP2.Identification of a cholesterol-binding pocket in inward rectifier K(+) (Kir) channels.Conformational changes during the gating of a potassium channel revealed by structural mass spectrometry.Identification of a binding motif in the S5 helix that confers cholesterol sensitivity to the TRPV1 ion channel.A long QT mutation substitutes cholesterol for phosphatidylinositol-4,5-bisphosphate in KCNQ1 channel regulation.Genetic defects in the hotspot of inwardly rectifying K(+) (Kir) channels and their metabolic consequences: a review Lovastatin-Induced Phosphatidylinositol-4-Phosphate 5-Kinase Diffusion from Microvilli Stimulates ROMK Channels.Distant cytosolic residues mediate a two-way molecular switch that controls the modulation of inwardly rectifying potassium (Kir) channels by cholesterol and phosphatidylinositol 4,5-bisphosphate (PI(4,5)P(2)).Identification of novel cholesterol-binding regions in Kir2 channels.Regulation of ion channels by membrane lipids.Structural Stringency of Cholesterol for Membrane Protein Function Utilizing Stereoisomers as Novel Tools: A Review.Molecular Dynamics Simulations of KirBac1.1 Mutants Reveal Global Gating Changes of Kir Channels.Lipid interaction sites on channels, transporters and receptors: Recent insights from molecular dynamics simulations.Desensitization mechanism in prokaryotic ligand-gated ion channel Cholesterol regulates prokaryotic Kir channel by direct binding to channel protein.Molecular dynamics simulations on the interaction of the transmembrane NavAb channel with cholesterol and lipids in the membrane.Silencing of Kir2 channels by caveolin-1: cross-talk with cholesterol.Molecular Dynamics Simulations of Kir2.2 Interactions with an Ensemble of Cholesterol Molecules

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P2860

Direct regulation of prokaryotic Kir channel by cholesterol.

http://www.wikidata.org/entity/Q37431875

description

article científic

@ca

article scientifique

@fr

articolo scientifico

@it

artigo científico

@pt

bilimsel makale

@tr

scientific article published on 09 September 2009

@en

vedecký článok

@sk

vetenskaplig artikel

@sv

videnskabelig artikel

@da

vědecký článek

@cs

name

Direct regulation of prokaryotic Kir channel by cholesterol.

@en

Direct regulation of prokaryotic Kir channel by cholesterol.

@nl

type

label

Direct regulation of prokaryotic Kir channel by cholesterol.

@en

Direct regulation of prokaryotic Kir channel by cholesterol.

@nl

prefLabel

Direct regulation of prokaryotic Kir channel by cholesterol.

@en

Direct regulation of prokaryotic Kir channel by cholesterol.

@nl

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JBC.M109.011221

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Journal of Biological Chemistry

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Direct regulation of prokaryotic Kir channel by cholesterol.

@en

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Avia Rosenhouse-Dantsker

http://www.w3.org/2001/XMLSchema#string

Colin G Nichols

http://www.w3.org/2001/XMLSchema#string

Decha Enkvetchakul

http://www.w3.org/2001/XMLSchema#string

Dev K Singh

http://www.w3.org/2001/XMLSchema#string

Irena Levitan

http://www.w3.org/2001/XMLSchema#string

P2860

The Structure of the Potassium Channel: Molecular Basis of K+ Conduction and Selectivity

Alterations in conserved Kir channel-PIP2 interactions underlie channelopathies

Regulation of sodium channel function by bilayer elasticity: the importance of hydrophobic coupling. Effects of Micelle-forming amphiphiles and cholesterol

Structural basis of inward rectification: cytoplasmic pore of the G protein-gated inward rectifier GIRK1 at 1.8 A resolution

Crystal structure of the potassium channel KirBac1.1 in the closed state

Crystal structure of a Kir3.1-prokaryotic Kir channel chimera

Functional expression of Kir2.x in human aortic endothelial cells: the dominant role of Kir2.2

Functional characterization of a prokaryotic Kir channel

International Union of Pharmacology. LIV. Nomenclature and molecular relationships of inwardly rectifying potassium channels

Sterol resistance in CHO cells traced to point mutation in SREBP cleavage-activating protein

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30727-30736

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scholarly article

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10.1074/JBC.M109.011221

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44

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284

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2009-09-09T00:00:00Z

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19740741

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2781626

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