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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
49
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pubmed:dateCreated |
1998-1-8
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pubmed:abstractText |
Disassembly of the coatomer from Golgi vesicles requires that the small GTP-binding protein ADP-ribosylation factor 1 (ARF1) hydrolyzes its bound GTP by the action of a GTPase-activating protein. In vitro, the binding of the ARF1 GTPase-activating protein to lipid vesicles and its activity on membrane-bound ARF1GTP are increased by diacylglycerols with monounsaturated acyl chains, such as those arising in vivo as secondary products from the hydrolysis of phosphatidylcholine by ARF-activated phospholipase D. Thus, the phospholipase D pathway may provide a feedback mechanism that promotes GTP hydrolysis on ARF1 and the consequent uncoating of vesicles.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/ADP-Ribosylation Factor 1,
http://linkedlifedata.com/resource/pubmed/chemical/ADP-Ribosylation Factors,
http://linkedlifedata.com/resource/pubmed/chemical/Carrier Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Diglycerides,
http://linkedlifedata.com/resource/pubmed/chemical/GTP Phosphohydrolases,
http://linkedlifedata.com/resource/pubmed/chemical/GTP-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/GTPase-Activating Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Guanosine Diphosphate,
http://linkedlifedata.com/resource/pubmed/chemical/Guanosine Triphosphate,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphatidylcholines,
http://linkedlifedata.com/resource/pubmed/chemical/Phospholipase D,
http://linkedlifedata.com/resource/pubmed/chemical/Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/diolein
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pubmed:status |
MEDLINE
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pubmed:month |
Dec
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pubmed:issn |
0021-9258
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
5
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pubmed:volume |
272
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
30848-51
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:9388229-ADP-Ribosylation Factor 1,
pubmed-meshheading:9388229-ADP-Ribosylation Factors,
pubmed-meshheading:9388229-Carrier Proteins,
pubmed-meshheading:9388229-Diglycerides,
pubmed-meshheading:9388229-Dose-Response Relationship, Drug,
pubmed-meshheading:9388229-Enzyme Activation,
pubmed-meshheading:9388229-Escherichia coli,
pubmed-meshheading:9388229-GTP Phosphohydrolases,
pubmed-meshheading:9388229-GTP-Binding Proteins,
pubmed-meshheading:9388229-GTPase-Activating Proteins,
pubmed-meshheading:9388229-Guanosine Diphosphate,
pubmed-meshheading:9388229-Guanosine Triphosphate,
pubmed-meshheading:9388229-Hydrolysis,
pubmed-meshheading:9388229-Models, Chemical,
pubmed-meshheading:9388229-Phosphatidylcholines,
pubmed-meshheading:9388229-Phospholipase D,
pubmed-meshheading:9388229-Proteins
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pubmed:year |
1997
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pubmed:articleTitle |
Activation of ADP-ribosylation factor 1 GTPase-activating protein by phosphatidylcholine-derived diacylglycerols.
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pubmed:affiliation |
CNRS, Institut de Pharmacologie Moléculaire et Cellulaire, 660 route des lucioles, 06560 Valbonne, France. antonny@unice.fr
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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