about
The caveolin proteinsCholesterol binds to synaptophysin and is required for biogenesis of synaptic vesiclesIdentification of a novel domain at the N terminus of caveolin-1 that controls rear polarization of the protein and caveolae formationThe sonic hedgehog receptor patched associates with caveolin-1 in cholesterol-rich microdomains of the plasma membraneBENE, a novel raft-associated protein of the MAL proteolipid family, interacts with caveolin-1 in human endothelial-like ECV304 cellsCaveolin-1-deficient mice show accelerated mammary gland development during pregnancy, premature lactation, and hyperactivation of the Jak-2/STAT5a signaling cascade.Cell-type and tissue-specific expression of caveolin-2. Caveolins 1 and 2 co-localize and form a stable hetero-oligomeric complex in vivoLigand-independent activation of oestrogen receptor alpha by caveolin-1Amyloid beta-protein stimulates trafficking of cholesterol and caveolin-1 from the plasma membrane to the Golgi complex in mouse primary astrocytesCharacterization of the molecular architecture of human caveolin-3 and interaction with the skeletal muscle ryanodine receptorExtraction of cholesterol with methyl-beta-cyclodextrin perturbs formation of clathrin-coated endocytic vesiclesStromal cell expression of caveolin-1 predicts outcome in breast cancerThe first 35 amino acids and fatty acylation sites determine the molecular targeting of endothelial nitric oxide synthase into the Golgi region of cells: a green fluorescent protein studyExpression of caveolin-1 and -2 in differentiating PC12 cells and dorsal root ganglion neurons: caveolin-2 is up-regulated in response to cell injuryCaveolae and Caveolin-1 Integrate Reverse Cholesterol Transport and Inflammation in AtherosclerosisGlutathione and mitochondriaMembrane domain formation-a key factor for targeted intracellular drug deliveryMitochondrial glutathione: features, regulation and role in diseaseThe fusion peptide of Semliki Forest virus associates with sterol-rich membrane domains.Cholesterol Effectively Blocks Entry of FlavivirusAre all n-3 polyunsaturated fatty acids created equal?p53 as a Regulator of Lipid Metabolism in CancerThe Mammalian Blood-Testis Barrier: Its Biology and RegulationCaveolin-2 localizes to the golgi complex but redistributes to plasma membrane, caveolae, and rafts when co-expressed with caveolin-1Association of phosphofructokinase-M with caveolin-3 in differentiated skeletal myotubes. Dynamic regulation by extracellular glucose and intracellular metabolitesThe MAL proteolipid restricts detergent-mediated membrane pore expansion and percolationCaveolae, plasma membrane microdomains for alpha-secretase-mediated processing of the amyloid precursor proteinRegulated localization of Rab18 to lipid droplets: effects of lipolytic stimulation and inhibition of lipid droplet catabolismGenes encoding human caveolin-1 and -2 are co-localized to the D7S522 locus (7q31.1), a known fragile site (FRA7G) that is frequently deleted in human cancersCholesterol depletion reduces apical transport capacity in epithelial Madin-Darby canine kidney cellsModulation of myoblast fusion by caveolin-3 in dystrophic skeletal muscle cells: implications for Duchenne muscular dystrophy and limb-girdle muscular dystrophy-1CCaveolin-1 and caveolin-2 expression in mouse macrophages. High density lipoprotein 3-stimulated secretion and a lack of significant subcellular co-localizationPTRF-Cavin, a conserved cytoplasmic protein required for caveola formation and functionCaveolin-3 associates with developing T-tubules during muscle differentiationMurine SR-BI, a high density lipoprotein receptor that mediates selective lipid uptake, is N-glycosylated and fatty acylated and colocalizes with plasma membrane caveolaeCaveolin-1 is enriched in the peroxisomal membrane of rat hepatocytesCaveolin-1 and mitochondrial alterations in regenerating rat liverApolipoprotein A-I induces translocation of cholesterol, phospholipid, and caveolin-1 to cytosol in rat astrocytesElevated cholesterol metabolism and bile acid synthesis in mice lacking membrane tyrosine kinase receptor FGFR4Caveolin-3 null mice show a loss of caveolae, changes in the microdomain distribution of the dystrophin-glycoprotein complex, and t-tubule abnormalities
P2860
Q21194854-8D25D554-F582-4A59-B2E3-EEDEE46D012EQ22011017-435E23E1-DC58-4738-85F6-2014ED025DFEQ23923938-1E154975-E9BB-4D9C-BC99-CF34BA4F5B59Q24291031-68402A03-4078-4461-9E56-D8DCE84F7BECQ24291104-B039DFC2-A4C9-41C0-BD06-BCF3EFDE1191Q24311717-E118DF27-8D9A-4193-B167-DCF1AFC89031Q24324547-2035AC70-798D-4FDC-82C9-190546F7413CQ24533468-8A2767A6-E001-48FB-A52B-0F1EAF3E0121Q24606835-95F07C92-0E35-46E4-9DC9-5E885045A947Q24608212-49B416B1-8644-4953-BE3E-314E27E9EFF4Q24657869-34F0D502-E418-46AD-911D-1D6A063DB188Q24658345-39E8605F-FD99-44E9-A11C-3945A7D7CE15Q24680049-E5367EAB-4C0F-4754-8BC6-F966F01B07A9Q24685904-C2DBF89B-CC25-47D1-AB05-7A0125E18F70Q26752101-6C3DD4BB-733B-4F1E-81F6-F17E70727F4BQ26865589-56B79974-B924-4C5B-B7A0-E59B3DB0E1B8Q26998461-81ADA145-F600-49E5-ACF5-7F3D96205E16Q27026521-3E7FB843-95D8-4261-80CB-A0A199E5C607Q27472848-DBF21843-B41F-41B6-AB5F-4D1B8ADDEDA2Q27486412-6F68884D-3459-4B30-85B9-B315EE18D806Q27497371-0BE8AA09-C931-4025-A05A-8644866A2715Q28079393-CFCCFFEA-908B-4E03-A72F-DB82900D1844Q28088573-A15C266B-183B-4669-995A-F0EFFDA8AC29Q28143130-0353060C-67C2-467E-9F57-3481F94D4A0BQ28245956-A6239A6E-FEF9-4EA9-8CD0-C7CDDAB34409Q28247030-64482802-4E0A-4634-91CC-790C8FAB2B48Q28268402-E2A64620-0B47-479C-B108-42495FE84729Q28275690-507EBFF3-4EC1-479B-8181-78A00C4F1048Q28287729-303FFF22-2E9E-4BFB-AFBA-5DF9E15E2006Q28367183-F99130E7-E8A5-437F-89A0-EDCB308F4559Q28506016-31B4DC29-CD8E-4190-8816-FB5D24BA3AD9Q28507990-7CE1F63E-EDC7-422C-93B9-33BD66BA61C1Q28511660-B343249B-99F3-4D18-A130-49FEB9C887D8Q28511690-E4D549C3-733D-4CCF-AAEE-EBF4026A6315Q28513709-BB25FCE5-D8D2-4F94-8D88-63762B05499BQ28568648-3E08510C-EE68-497E-87FC-AF558AE1D8B6Q28576372-23EFE73D-7408-40AF-A68B-33CD5C8EECECQ28576875-8F06DB8B-B8E4-4F11-94BE-4D82F2F087E4Q28590891-1A06E2CA-5C46-4C7E-9235-33AC5DF9CA59Q28592366-109CA973-3372-43F1-B768-E31574DCCF8F
P2860
description
1995 nî lūn-bûn
@nan
1995 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած
@hyw
1995 թվականի հոտեմբերին հրատարակված գիտական հոդված
@hy
1995年の論文
@ja
1995年論文
@yue
1995年論文
@zh-hant
1995年論文
@zh-hk
1995年論文
@zh-mo
1995年論文
@zh-tw
1995年论文
@wuu
name
VIP21/caveolin is a cholesterol-binding protein
@ast
VIP21/caveolin is a cholesterol-binding protein
@en
VIP21/caveolin is a cholesterol-binding protein
@nl
type
label
VIP21/caveolin is a cholesterol-binding protein
@ast
VIP21/caveolin is a cholesterol-binding protein
@en
VIP21/caveolin is a cholesterol-binding protein
@nl
prefLabel
VIP21/caveolin is a cholesterol-binding protein
@ast
VIP21/caveolin is a cholesterol-binding protein
@en
VIP21/caveolin is a cholesterol-binding protein
@nl
P2093
P2860
P3181
P356
P1476
VIP21/caveolin is a cholesterol-binding protein
@en
P2093
R Schreiner
T V Kurzchalia
P2860
P304
P3181
P356
10.1073/PNAS.92.22.10339
P407
P50
P577
1995-10-24T00:00:00Z