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rdf:type |
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lifeskim:mentions |
umls-concept:C0004083,
umls-concept:C0019629,
umls-concept:C0030685,
umls-concept:C0030956,
umls-concept:C0034115,
umls-concept:C0086597,
umls-concept:C0391871,
umls-concept:C0680255,
umls-concept:C1148916,
umls-concept:C1283071,
umls-concept:C1417898,
umls-concept:C1706853,
umls-concept:C1864009,
umls-concept:C1963578
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pubmed:issue |
18
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pubmed:dateCreated |
2000-2-14
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pubmed:abstractText |
Newly synthesised peptide-receptive major histocompatibility complex (MHC) class I molecules form a transient loading complex in the endoplasmic reticulum with the transporter associated with antigen processing (TAP) and a set of accessory proteins. Binding of peptide to the MHC class I molecule is necessary for dissociation of the MHC class I molecule from the complex with TAP, but other components of the complex might also be involved. To investigate the role of TAP in this process, mutations that block nucleotide binding were introduced into the ATP-binding site of TAP.
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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/ATP-Binding Cassette Transporters,
http://linkedlifedata.com/resource/pubmed/chemical/Adenosine Triphosphate,
http://linkedlifedata.com/resource/pubmed/chemical/HLA-A2 Antigen,
http://linkedlifedata.com/resource/pubmed/chemical/HLA-B Antigens,
http://linkedlifedata.com/resource/pubmed/chemical/HLA-B5 antigen,
http://linkedlifedata.com/resource/pubmed/chemical/Histocompatibility Antigens Class I,
http://linkedlifedata.com/resource/pubmed/chemical/Peptide Fragments,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Fusion Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/TAP1 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/TAP2 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Tap1 protein, rat,
http://linkedlifedata.com/resource/pubmed/chemical/Tap2 protein, rat
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pubmed:status |
MEDLINE
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pubmed:month |
Sep
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pubmed:issn |
0960-9822
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
23
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pubmed:volume |
9
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
999-1008
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pubmed:dateRevised |
2011-11-17
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pubmed:meshHeading |
pubmed-meshheading:10508608-ATP-Binding Cassette Transporters,
pubmed-meshheading:10508608-Adenosine Triphosphate,
pubmed-meshheading:10508608-Allosteric Regulation,
pubmed-meshheading:10508608-Animals,
pubmed-meshheading:10508608-Antigen Presentation,
pubmed-meshheading:10508608-Binding Sites,
pubmed-meshheading:10508608-HLA-A2 Antigen,
pubmed-meshheading:10508608-HLA-B Antigens,
pubmed-meshheading:10508608-Histocompatibility Antigens Class I,
pubmed-meshheading:10508608-Humans,
pubmed-meshheading:10508608-Mutagenesis, Site-Directed,
pubmed-meshheading:10508608-Peptide Fragments,
pubmed-meshheading:10508608-Protein Binding,
pubmed-meshheading:10508608-Rats,
pubmed-meshheading:10508608-Recombinant Fusion Proteins
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pubmed:year |
1999
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pubmed:articleTitle |
Nucleotide binding by TAP mediates association with peptide and release of assembled MHC class I molecules.
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pubmed:affiliation |
Institute for Genetics University of Cologne D-50674, Cologne, Germany. Knittler@uni-koeln.de
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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