Cholesterol interaction with proteins that partition into membrane domains: an overview.
about
The Relationship between Glycan Binding and Direct Membrane Interactions in Vibrio cholerae Cytolysin, a Channel-forming Toxin.Fluorescence image screening for chemical compounds modifying cholesterol metabolism and distribution.Cavin family proteins and the assembly of caveolae.Fusion-competent state induced by a C-terminal HIV-1 fusion peptide in cholesterol-rich membranes.Statins impair glucose uptake in tumor cellsMultiple cholesterol recognition/interaction amino acid consensus (CRAC) motifs in cytosolic C tail of Slo1 subunit determine cholesterol sensitivity of Ca2+- and voltage-gated K+ (BK) channelsIn Vivo Linking of Membrane Lipids and the Anion Transporter Band 3 with Thiourea-modified Amphiphilic Lipid Probes.A mirror code for protein-cholesterol interactions in the two leaflets of biological membranes.How cholesterol interacts with membrane proteins: an exploration of cholesterol-binding sites including CRAC, CARC, and tilted domains.Cholesterol as a co-solvent and a ligand for membrane proteins.The importance of claudin-7 palmitoylation on membrane subdomain localization and metastasis-promoting activities.Disclosure of cholesterol recognition motifs in transmembrane domains of the human nicotinic acetylcholine receptor.All-or-none versus graded: single-vesicle analysis reveals lipid composition effects on membrane permeabilization.Cholesterol accelerates the binding of Alzheimer's β-amyloid peptide to ganglioside GM1 through a universal hydrogen-bond-dependent sterol tuning of glycolipid conformation.The tumor necrosis factor receptor stalk regions define responsiveness to soluble versus membrane-bound ligand.The dynamic binding of cholesterol to the multiple sites of C99: as revealed by coarse-grained and all-atom simulations.
P2860
Q30379698-A94536FC-9D8B-4559-8A6E-683AC1661A8BQ34001443-BAC28F07-2AF2-417B-9260-AB64806B5E04Q34469647-A6ED3672-1924-43AB-BE88-D1B7C9335D14Q35091283-3A7357AE-8B80-43BD-BD9E-E43D5909302CQ35949773-8E4C24FC-2759-40E4-88D5-34F6AE6F6C5EQ36016953-3ECB9804-7AB0-4ADA-9F66-0501743A6A16Q36329649-0B4C8388-554C-44E7-BA6C-B728C0A4DEF7Q36621319-12EE30B1-AA4D-4124-B6F8-34E8A9627308Q38085605-574E55DF-2C58-46FF-B296-B15523C0C105Q38155118-837ACB43-4579-4BA9-ABE4-91AEB0D5D5BAQ38866280-60D579B0-9E03-4431-B81A-2694C043D150Q39120707-B95F317E-B3EC-4AA6-BF54-F8F91CCE225EQ41152752-34A3DCFB-4318-4863-89FD-35B602E482E2Q41771186-B33AF0D6-F2B3-4895-832A-2C39F4C1474BQ42323234-177EDFD9-21A3-4079-8527-5C1F6AF8C7CBQ48049422-CFE80DAB-48FD-4FE9-BCBB-34F2E8623AFE
P2860
Cholesterol interaction with proteins that partition into membrane domains: an overview.
description
article científic
@ca
article scientifique
@fr
articolo scientifico
@it
artigo científico
@pt
bilimsel makale
@tr
scientific article published on January 2010
@en
vedecký článok
@sk
vetenskaplig artikel
@sv
videnskabelig artikel
@da
vědecký článek
@cs
name
Cholesterol interaction with proteins that partition into membrane domains: an overview.
@en
Cholesterol interaction with proteins that partition into membrane domains: an overview.
@nl
type
label
Cholesterol interaction with proteins that partition into membrane domains: an overview.
@en
Cholesterol interaction with proteins that partition into membrane domains: an overview.
@nl
prefLabel
Cholesterol interaction with proteins that partition into membrane domains: an overview.
@en
Cholesterol interaction with proteins that partition into membrane domains: an overview.
@nl
P2093
P1476
Cholesterol interaction with proteins that partition into membrane domains: an overview.
@en
P2093
Annick Thomas
Raquel F Epand
Richard M Epand
Robert Brasseur
P304
P356
10.1007/978-90-481-8622-8_9
P577
2010-01-01T00:00:00Z