| pubmed-article:10698930 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:10698930 | lifeskim:mentions | umls-concept:C0019630 | lld:lifeskim |
| pubmed-article:10698930 | lifeskim:mentions | umls-concept:C2717970 | lld:lifeskim |
| pubmed-article:10698930 | lifeskim:mentions | umls-concept:C1254042 | lld:lifeskim |
| pubmed-article:10698930 | pubmed:issue | 5 | lld:pubmed |
| pubmed-article:10698930 | pubmed:dateCreated | 2000-4-26 | lld:pubmed |
| pubmed-article:10698930 | pubmed:abstractText | Major histocompatibility complex (MHC) class II molecules bind and present to CD4(+) T cells peptides derived from endocytosed antigens. Class II molecules associate in the endoplasmic reticulum with invariant chain (Ii), which (i) mediates the delivery of the class II-Ii complexes into the endocytic compartments where the antigenic peptides are generated; and (ii) blocks the peptide-binding site of the class II molecules until they reach their destination. Once there, Ii must be removed to allow peptide binding. The bulk of Ii-class II complexes reach late endocytic compartments where Ii is eliminated in a reaction in which the cysteine protease cathepsin S and the accessory molecule H-2DM play an essential role. Here, we here show that Ii is also eliminated in early endosomal compartments without the intervention of cysteine proteases or H-2DM. The Ii-free class II molecules generated by this alternative mechanism first bind high molecular weight polypeptides and then mature into peptide-loaded complexes. | lld:pubmed |
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| pubmed-article:10698930 | pubmed:language | eng | lld:pubmed |
| pubmed-article:10698930 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10698930 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:10698930 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:10698930 | pubmed:month | Mar | lld:pubmed |
| pubmed-article:10698930 | pubmed:issn | 0261-4189 | lld:pubmed |
| pubmed-article:10698930 | pubmed:author | pubmed-author:PloeghH LHL | lld:pubmed |
| pubmed-article:10698930 | pubmed:author | pubmed-author:ChapmanH AHA | lld:pubmed |
| pubmed-article:10698930 | pubmed:author | pubmed-author:ShiG PGP | lld:pubmed |
| pubmed-article:10698930 | pubmed:author | pubmed-author:VilladangosJ... | lld:pubmed |
| pubmed-article:10698930 | pubmed:author | pubmed-author:DriessenCC | lld:pubmed |
| pubmed-article:10698930 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:10698930 | pubmed:day | 1 | lld:pubmed |
| pubmed-article:10698930 | pubmed:volume | 19 | lld:pubmed |
| pubmed-article:10698930 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:10698930 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:10698930 | pubmed:pagination | 882-91 | lld:pubmed |
| pubmed-article:10698930 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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| pubmed-article:10698930 | pubmed:meshHeading | pubmed-meshheading:10698930... | lld:pubmed |
| pubmed-article:10698930 | pubmed:meshHeading | pubmed-meshheading:10698930... | lld:pubmed |
| pubmed-article:10698930 | pubmed:meshHeading | pubmed-meshheading:10698930... | lld:pubmed |
| pubmed-article:10698930 | pubmed:meshHeading | pubmed-meshheading:10698930... | lld:pubmed |
| pubmed-article:10698930 | pubmed:meshHeading | pubmed-meshheading:10698930... | lld:pubmed |
| pubmed-article:10698930 | pubmed:meshHeading | pubmed-meshheading:10698930... | lld:pubmed |
| pubmed-article:10698930 | pubmed:year | 2000 | lld:pubmed |
| pubmed-article:10698930 | pubmed:articleTitle | Early endosomal maturation of MHC class II molecules independently of cysteine proteases and H-2DM. | lld:pubmed |
| pubmed-article:10698930 | pubmed:affiliation | Department of Pathology, Harvard Medical School, Boston, MA 02115, USA. | lld:pubmed |
| pubmed-article:10698930 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:10698930 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:10698930 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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