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Cholesterol binding to ion channels

Cholesterol binding to ion channels

http://www.wikidata.org/entity/Q29036398

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Specialized Functional Diversity and Interactions of the Na,K-ATPase Susceptibility of outer hair cells to cholesterol chelator 2-hydroxypropyl-β-cyclodextrine is prestin-dependent Using Sterol Substitution to Probe the Role of Membrane Domains in Membrane Functions.A Pore Idea: the ion conduction pathway of TMEM16/ANO proteins is composed partly of lipid Computational investigation of cholesterol binding sites on mitochondrial VDAC.Cholesterol in brain disease: sometimes determinant and frequently implicated.Molecular Properties of Globin Channels and Pores: Role of Cholesterol in Ligand Binding and Movement.Multidimensional Liquid Chromatography Coupled with Tandem Mass Spectrometry for Identification of Bioactive Fatty Acyl Derivatives Whole-GUV patch-clamping.Cholesterol regulates polymodal sensory transduction in Müller glia.Structural Stringency of Cholesterol for Membrane Protein Function Utilizing Stereoisomers as Novel Tools: A Review.Membrane Perfusion of Hydrophobic Substances Around Channels Embedded in the Contact Bubble Bilayer.Cholesterol modulates open probability and desensitization of NMDA receptors.Caveolar disruption causes contraction of rat femoral arteries via reduced basal NO release and subsequent closure of BKCa channels.The conserved tyrosine residue 940 plays a key structural role in membrane interaction of Bordetella adenylate cyclase toxin.A cholesterol-binding domain in STIM1 modulates STIM1-Orai1 physical and functional interactions.Myocyte membrane and microdomain modifications in diabetes: determinants of ischemic tolerance and cardioprotection.Identification of Two New Cholesterol Interaction Sites on the A2A Adenosine Receptor.Lipids at membrane contact sites: cell signaling and ion transport.Reduced membrane cholesterol after chronic hypoxia limits Orai1-mediated pulmonary endothelial Ca2+ entry.Membrane cholesterol depletion as a trigger of Nav1.9 channel-mediated inflammatory pain.7DHC-induced changes of Kv1.3 operation contributes to modified T cell function in Smith-Lemli-Opitz syndrome.Membrane lipid rafts are disturbed in the response of rat skeletal muscle to short-term disuse.Regulation of Kir2.1 Function Under Shear Stress and Cholesterol Loading.Molecular Dynamics Simulations of Kir2.2 Interactions with an Ensemble of Cholesterol Molecules Cytotoxic activity of Kingella kingae RtxA toxin depends on post-translational acylation of lysine residues and cholesterol binding

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Cholesterol binding to ion channels

http://www.wikidata.org/entity/Q29036398

description

2014 nî lūn-bûn

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2014 թուականին հրատարակուած գիտական յօդուած

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2014 թվականին հրատարակված գիտական հոդված

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2014年の論文

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2014年論文

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2014年論文

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2014年論文

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2014年論文

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2014年論文

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2014年论文

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name

Cholesterol binding to ion channels

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Cholesterol binding to ion channels

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Cholesterol binding to ion channels

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Cholesterol binding to ion channels

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FPHYS.2014.00065

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Frontiers in Physiology

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Cholesterol binding to ion channels

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Avia Rosenhouse-Dantsker

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Dev K. Singh

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

Irena Levitan

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Direct and specific activation of human inward rectifier K+ channels by membrane phosphatidylinositol 4,5-bisphosphate

NPC2 facilitates bidirectional transfer of cholesterol between NPC1 and lipid bilayers, a step in cholesterol egress from lysosomes

X-ray structure of dopamine transporter elucidates antidepressant mechanism

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

High-resolution crystal structure of an engineered human beta2-adrenergic G protein-coupled receptor

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

A Specific Cholesterol Binding Site Is Established by the 2.8 Å Structure of the Human β2-Adrenergic Receptor

Crystal structure of the eukaryotic light-driven proton-pumping rhodopsin, Acetabularia rhodopsin II, from marine alga

Structural Basis for Allosteric Regulation of GPCRs by Sodium Ions

Structural Features for Functional Selectivity at Serotonin Receptors

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scholarly article

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1367254

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10.3389/FPHYS.2014.00065

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5

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2014-01-01T00:00:00Z

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260684473

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24616704

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3935357

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