| pubmed-article:11250152 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:11250152 | lifeskim:mentions | umls-concept:C0005528 | lld:lifeskim |
| pubmed-article:11250152 | lifeskim:mentions | umls-concept:C0205245 | lld:lifeskim |
| pubmed-article:11250152 | lifeskim:mentions | umls-concept:C1417898 | lld:lifeskim |
| pubmed-article:11250152 | lifeskim:mentions | umls-concept:C1864009 | lld:lifeskim |
| pubmed-article:11250152 | lifeskim:mentions | umls-concept:C0034115 | lld:lifeskim |
| pubmed-article:11250152 | lifeskim:mentions | umls-concept:C1511572 | lld:lifeskim |
| pubmed-article:11250152 | lifeskim:mentions | umls-concept:C1711351 | lld:lifeskim |
| pubmed-article:11250152 | lifeskim:mentions | umls-concept:C1707511 | lld:lifeskim |
| pubmed-article:11250152 | lifeskim:mentions | umls-concept:C0871161 | lld:lifeskim |
| pubmed-article:11250152 | pubmed:issue | 4 | lld:pubmed |
| pubmed-article:11250152 | pubmed:dateCreated | 2001-3-16 | lld:pubmed |
| pubmed-article:11250152 | pubmed:abstractText | The transporter associated with antigen processing (TAP) consists of two polypeptides, TAP1 and TAP2. TAP delivers peptides into the ER and forms a "loading complex" with MHC class I molecules and accessory proteins. Our previous experiments indicated that nucleotide binding to TAP plays a critical role in the uptake of peptide and the release of assembled class I molecules. To investigate whether the conserved nucleotide binding domains (NBDs) of TAP1 and TAP2 are functionally equivalent, we created TAP variants in which only one of the two ATP binding sites was mutated. | lld:pubmed |
| pubmed-article:11250152 | pubmed:language | eng | lld:pubmed |
| pubmed-article:11250152 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11250152 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:11250152 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11250152 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11250152 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11250152 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11250152 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11250152 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11250152 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11250152 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:11250152 | pubmed:month | Feb | lld:pubmed |
| pubmed-article:11250152 | pubmed:issn | 0960-9822 | lld:pubmed |
| pubmed-article:11250152 | pubmed:author | pubmed-author:AlbertsPP | lld:pubmed |
| pubmed-article:11250152 | pubmed:author | pubmed-author:HowardJ CJC | lld:pubmed |
| pubmed-article:11250152 | pubmed:author | pubmed-author:DeversonE VEV | lld:pubmed |
| pubmed-article:11250152 | pubmed:author | pubmed-author:KnittlerM RMR | lld:pubmed |
| pubmed-article:11250152 | pubmed:author | pubmed-author:DaumkeOO | lld:pubmed |
| pubmed-article:11250152 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:11250152 | pubmed:day | 20 | lld:pubmed |
| pubmed-article:11250152 | pubmed:volume | 11 | lld:pubmed |
| pubmed-article:11250152 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:11250152 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:11250152 | pubmed:pagination | 242-51 | lld:pubmed |
| pubmed-article:11250152 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
| pubmed-article:11250152 | pubmed:meshHeading | pubmed-meshheading:11250152... | lld:pubmed |
| pubmed-article:11250152 | pubmed:meshHeading | pubmed-meshheading:11250152... | lld:pubmed |
| pubmed-article:11250152 | pubmed:meshHeading | pubmed-meshheading:11250152... | lld:pubmed |
| pubmed-article:11250152 | pubmed:meshHeading | pubmed-meshheading:11250152... | lld:pubmed |
| pubmed-article:11250152 | pubmed:meshHeading | pubmed-meshheading:11250152... | lld:pubmed |
| pubmed-article:11250152 | pubmed:meshHeading | pubmed-meshheading:11250152... | lld:pubmed |
| pubmed-article:11250152 | pubmed:meshHeading | pubmed-meshheading:11250152... | lld:pubmed |
| pubmed-article:11250152 | pubmed:meshHeading | pubmed-meshheading:11250152... | lld:pubmed |
| pubmed-article:11250152 | pubmed:meshHeading | pubmed-meshheading:11250152... | lld:pubmed |
| pubmed-article:11250152 | pubmed:meshHeading | pubmed-meshheading:11250152... | lld:pubmed |
| pubmed-article:11250152 | pubmed:meshHeading | pubmed-meshheading:11250152... | lld:pubmed |
| pubmed-article:11250152 | pubmed:year | 2001 | lld:pubmed |
| pubmed-article:11250152 | pubmed:articleTitle | Distinct functional properties of the TAP subunits coordinate the nucleotide-dependent transport cycle. | lld:pubmed |
| pubmed-article:11250152 | pubmed:affiliation | Institute for Genetics, University of Cologne, D-50674, Cologne, Germany. | lld:pubmed |
| pubmed-article:11250152 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:11250152 | pubmed:publicationType | Comparative Study | lld:pubmed |
| pubmed-article:11250152 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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