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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
4
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pubmed:dateCreated |
1993-3-8
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pubmed:databankReference |
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pubmed:abstractText |
N-Ethylmaleimide-sensitive fusion protein (NSF) is an essential component for protein transport between Golgi cisternae. Sequence analysis and proteolytic dissection reveal that NSF contains two tandem "ATP domains," each containing the consensus sequence for the binding of nucleotide. When Escherichia coli-produced Chinese hamster ovary NSF is purified, it exhibits a low, but significant, ATPase activity. The ATPase activity of NSF is sensitive to N-ethylmaleimide and influenced by monoclonal antibodies against recombinant NSF.
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pubmed:grant |
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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/Adenosine Triphosphatases,
http://linkedlifedata.com/resource/pubmed/chemical/Adenosine Triphosphate,
http://linkedlifedata.com/resource/pubmed/chemical/Antibodies, Monoclonal,
http://linkedlifedata.com/resource/pubmed/chemical/Carrier Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Ethylmaleimide,
http://linkedlifedata.com/resource/pubmed/chemical/Macromolecular Substances,
http://linkedlifedata.com/resource/pubmed/chemical/N-Ethylmaleimide-Sensitive Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Peptide Fragments,
http://linkedlifedata.com/resource/pubmed/chemical/Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Vesicular Transport Proteins
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pubmed:status |
MEDLINE
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pubmed:month |
Feb
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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 |
268
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
2662-6
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:8428942-Adenosine Triphosphatases,
pubmed-meshheading:8428942-Adenosine Triphosphate,
pubmed-meshheading:8428942-Amino Acid Sequence,
pubmed-meshheading:8428942-Animals,
pubmed-meshheading:8428942-Antibodies, Monoclonal,
pubmed-meshheading:8428942-Binding Sites,
pubmed-meshheading:8428942-Biological Transport,
pubmed-meshheading:8428942-CHO Cells,
pubmed-meshheading:8428942-Carrier Proteins,
pubmed-meshheading:8428942-Cricetinae,
pubmed-meshheading:8428942-Ethylmaleimide,
pubmed-meshheading:8428942-Golgi Apparatus,
pubmed-meshheading:8428942-Macromolecular Substances,
pubmed-meshheading:8428942-Molecular Sequence Data,
pubmed-meshheading:8428942-N-Ethylmaleimide-Sensitive Proteins,
pubmed-meshheading:8428942-Peptide Fragments,
pubmed-meshheading:8428942-Proteins,
pubmed-meshheading:8428942-Vesicular Transport Proteins
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pubmed:year |
1993
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pubmed:articleTitle |
Domain structure of an N-ethylmaleimide-sensitive fusion protein involved in vesicular transport.
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pubmed:affiliation |
Program in Cellular Biochemistry and Biophysics, Rockefeller Research Laboratory, Sloan-Kettering Institute, New York, New York 10021.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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