| pubmed-article:12200052 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:12200052 | lifeskim:mentions | umls-concept:C0014239 | lld:lifeskim |
| pubmed-article:12200052 | lifeskim:mentions | umls-concept:C0019629 | lld:lifeskim |
| pubmed-article:12200052 | lifeskim:mentions | umls-concept:C0439855 | lld:lifeskim |
| pubmed-article:12200052 | lifeskim:mentions | umls-concept:C1149098 | lld:lifeskim |
| pubmed-article:12200052 | lifeskim:mentions | umls-concept:C1952609 | lld:lifeskim |
| pubmed-article:12200052 | lifeskim:mentions | umls-concept:C1708715 | lld:lifeskim |
| pubmed-article:12200052 | lifeskim:mentions | umls-concept:C2346689 | lld:lifeskim |
| pubmed-article:12200052 | pubmed:issue | 3-4 | lld:pubmed |
| pubmed-article:12200052 | pubmed:dateCreated | 2002-8-29 | lld:pubmed |
| pubmed-article:12200052 | pubmed:abstractText | MHC class I molecules are loaded with peptides that mostly originate from the degradation of cytosolic protein antigens and that are translocated across the endoplasmic reticulum (ER) membrane by the transporter associated with antigen processing (TAP). The ER-resident molecule tapasin (Tpn) is uniquely dedicated to tether class I molecules jointly with the chaperone calreticulin (Crt) and the oxidoreductase ERp57 to TAP. As learned from the study of a Tpn-deficient cell line and from mice harboring a disrupted Tpn gene, the transient association of class I molecules with Tpn and TAP is critically important for the stabilization of class I molecules and the optimization of the peptide cargo presented to cytotoxic T cells. The different functions of molecular domains of Tpn and the highly coordinated formation of the TAP-associated peptide loading complex will also be discussed in this review. | lld:pubmed |
| pubmed-article:12200052 | pubmed:language | eng | lld:pubmed |
| pubmed-article:12200052 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12200052 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:12200052 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:12200052 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:12200052 | pubmed:month | Oct | lld:pubmed |
| pubmed-article:12200052 | pubmed:issn | 0161-5890 | lld:pubmed |
| pubmed-article:12200052 | pubmed:author | pubmed-author:TaoSS | lld:pubmed |
| pubmed-article:12200052 | pubmed:author | pubmed-author:MomburgFF | lld:pubmed |
| pubmed-article:12200052 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:12200052 | pubmed:volume | 39 | lld:pubmed |
| pubmed-article:12200052 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:12200052 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:12200052 | pubmed:pagination | 217-33 | lld:pubmed |
| pubmed-article:12200052 | pubmed:dateRevised | 2008-11-21 | lld:pubmed |
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| pubmed-article:12200052 | pubmed:meshHeading | pubmed-meshheading:12200052... | lld:pubmed |
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| pubmed-article:12200052 | pubmed:meshHeading | pubmed-meshheading:12200052... | lld:pubmed |
| pubmed-article:12200052 | pubmed:year | 2002 | lld:pubmed |
| pubmed-article:12200052 | pubmed:articleTitle | Tapasin-the keystone of the loading complex optimizing peptide binding by MHC class I molecules in the endoplasmic reticulum. | lld:pubmed |
| pubmed-article:12200052 | pubmed:affiliation | Department of Molecular Immunology, German Cancer Research Center (DKFZ), Im Neuenheimer Feld 280, 69120 Heidelberg, Germany. f.momburg@dkfz.de | lld:pubmed |
| pubmed-article:12200052 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:12200052 | pubmed:publicationType | Review | lld:pubmed |
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