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VIP21/caveolin is a cholesterol-binding protein
scientific article
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scholarly article
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title
VIP21/caveolin is a cholesterol-binding protein
(English)
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author
Kai Simons
object named as
K Simons
series ordinal
6
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author name string
M Murata
series ordinal
1
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J Peränen
series ordinal
2
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R Schreiner
series ordinal
3
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F Wieland
series ordinal
4
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T V Kurzchalia
series ordinal
5
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language of work or name
English
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publication date
24 October 1995
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published in
Proceedings of the National Academy of Sciences of the United States of America
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volume
92
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issue
22
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page(s)
10339-43
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cites work
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Interactions between saturated acyl chains confer detergent resistance on lipids and glycosylphosphatidylinositol (GPI)-anchored proteins: GPI-anchored proteins in liposomes and cells show similar behavior
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Cholesterol controls the clustering of the glycophospholipid-anchored membrane receptor for 5-methyltetrahydrofolate
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A RAPID METHOD OF TOTAL LIPID EXTRACTION AND PURIFICATION
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The sequence of human caveolin reveals identity with VIP21, a component of transport vesicles
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Sorting of GPI-anchored proteins to glycolipid-enriched membrane subdomains during transport to the apical cell surface
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Caveolin, a protein component of caveolae membrane coats
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Caveolin moves from caveolae to the Golgi apparatus in response to cholesterol oxidation
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VIP21-caveolin, a membrane protein constituent of the caveolar coat, oligomerizes in vivo and in vitro
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Lowering the cholesterol content of MA104 cells inhibits receptor-mediated transport of folate
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Potocytosis: Sequestration and Transport of Small Molecules by Caveolae
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Detergent-insoluble glycolipid microdomains in lymphocytes in the absence of caveolae.
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30 May 2018
Sterol and squalene carrier protein interactions with fluorescent delta 5,7,9(11)-cholestatrien-3 beta-ol.
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Tyrosine phosphorylation of a 22-kDa protein is correlated with transformation by Rous sarcoma virus
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VIP21, a 21-kD membrane protein is an integral component of trans-Golgi-network-derived transport vesicles
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PubMed Central
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30 May 2018
Each caveola contains multiple glycosyl-phosphatidylinositol-anchored membrane proteins
1 reference
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PubMed Central
reference URL
https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=40792
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Non-coated membrane invaginations are involved in binding and internalization of cholera and tetanus toxins
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PubMed
reference URL
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retrieved
12 December 2020
based on heuristic
inferred from PubMed ID database lookup
Ultrastructural localization of gangliosides; GM1 is concentrated in caveolae
1 reference
stated in
PubMed
reference URL
https://pubmed.ncbi.nlm.nih.gov/7479780
retrieved
12 December 2020
based on heuristic
inferred from PubMed ID database lookup
Selective binding of cholesterol by recombinant fatty acid binding proteins
1 reference
stated in
PubMed
reference URL
https://pubmed.ncbi.nlm.nih.gov/7479780
retrieved
12 December 2020
based on heuristic
inferred from PubMed ID database lookup
Identifiers
DOI
10.1073/PNAS.92.22.10339
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
4072516
ADS bibcode
1995PNAS...9210339M
0 references
OpenCitations bibliographic resource ID
4072516
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
4072516
PMCID
40792
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
4072516
PubMed ID
7479780
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
4072516
ResearchGate publication ID
15718881
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