pubmed-article:10887053 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:10887053 | lifeskim:mentions | umls-concept:C0086418 | lld:lifeskim |
pubmed-article:10887053 | lifeskim:mentions | umls-concept:C0023516 | lld:lifeskim |
pubmed-article:10887053 | lifeskim:mentions | umls-concept:C0022688 | lld:lifeskim |
pubmed-article:10887053 | lifeskim:mentions | umls-concept:C0431085 | lld:lifeskim |
pubmed-article:10887053 | lifeskim:mentions | umls-concept:C1853126 | lld:lifeskim |
pubmed-article:10887053 | lifeskim:mentions | umls-concept:C1415585 | lld:lifeskim |
pubmed-article:10887053 | lifeskim:mentions | umls-concept:C0678836 | lld:lifeskim |
pubmed-article:10887053 | lifeskim:mentions | umls-concept:C0449297 | lld:lifeskim |
pubmed-article:10887053 | lifeskim:mentions | umls-concept:C2347946 | lld:lifeskim |
pubmed-article:10887053 | pubmed:issue | 1 | lld:pubmed |
pubmed-article:10887053 | pubmed:dateCreated | 2001-1-26 | lld:pubmed |
pubmed-article:10887053 | pubmed:abstractText | HLA-E (human leucocyte antigen-E) is a conserved class I major histocompatibility molecule which has only limited polymorphism. It binds to the leader peptide derived from the polymorphic classical major histocompatibility molecules HLA-A, HLA-B and HLA-C. This peptide binding is highly specific and stabilizes the HLA-E protein, allowing it to migrate to the cell surface. A functioning TAP (transporter associated with antigen processing) molecule is required to transport these peptides into the endoplasmic reticulum, where they can interact with HLA-E. HLA-E then migrates to the cell surface, where it interacts with CD94/NKG2A receptors on natural killer cells. This interaction inhibits natural killer cell-mediated lysis of a cell displaying HLA-E. If the leader peptide is not present in the endoplasmic reticulum, HLA-E is unstable and is degraded before it reaches the cell surface. In damaged cells, such as virally infected or tumour cells, down-regulation of HLA-A, HLA-B and HLA-C production or inhibition of TAP prevents stabilization of HLA-E by the leader peptide. Under these circumstances, HLA-E does not reach the cell surface and the cell is then vulnerable to lysis by natural killer cells. The molecular mechanisms underlying this function of HLA-E have been revealed by crystallographic studies of the structure of HLA-E. | lld:pubmed |
pubmed-article:10887053 | pubmed:language | eng | lld:pubmed |
pubmed-article:10887053 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:10887053 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:10887053 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:10887053 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:10887053 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:10887053 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:10887053 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:10887053 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:10887053 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:10887053 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:10887053 | pubmed:month | Jul | lld:pubmed |
pubmed-article:10887053 | pubmed:issn | 0143-5221 | lld:pubmed |
pubmed-article:10887053 | pubmed:author | pubmed-author:O'CallaghanC... | lld:pubmed |
pubmed-article:10887053 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:10887053 | pubmed:volume | 99 | lld:pubmed |
pubmed-article:10887053 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:10887053 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:10887053 | pubmed:pagination | 9-17 | lld:pubmed |
pubmed-article:10887053 | pubmed:dateRevised | 2008-11-21 | lld:pubmed |
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pubmed-article:10887053 | pubmed:year | 2000 | lld:pubmed |
pubmed-article:10887053 | pubmed:articleTitle | Molecular basis of human natural killer cell recognition of HLA-E (human leucocyte antigen-E) and its relevance to clearance of pathogen-infected and tumour cells. | lld:pubmed |
pubmed-article:10887053 | pubmed:affiliation | MRC Human Immunology Unit, Nuffield Department of Clinical Medicine, Institute of Molecular Medicine, John Radcliffe Hospital, Oxford OX3 9DS, UK. chrisoc@itsa.ucsf.edu | lld:pubmed |
pubmed-article:10887053 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:10887053 | pubmed:publicationType | Review | lld:pubmed |
pubmed-article:10887053 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:10887053 | lld:pubmed |