| pubmed-article:16537370 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:16537370 | lifeskim:mentions | umls-concept:C0017355 | lld:lifeskim |
| pubmed-article:16537370 | lifeskim:mentions | umls-concept:C0208355 | lld:lifeskim |
| pubmed-article:16537370 | lifeskim:mentions | umls-concept:C0233820 | lld:lifeskim |
| pubmed-article:16537370 | lifeskim:mentions | umls-concept:C0023688 | lld:lifeskim |
| pubmed-article:16537370 | lifeskim:mentions | umls-concept:C0079411 | lld:lifeskim |
| pubmed-article:16537370 | lifeskim:mentions | umls-concept:C1513371 | lld:lifeskim |
| pubmed-article:16537370 | pubmed:issue | 12 | lld:pubmed |
| pubmed-article:16537370 | pubmed:dateCreated | 2006-3-22 | lld:pubmed |
| pubmed-article:16537370 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16537370 | pubmed:abstractText | Most class I MHC ligands are generated from the vast majority of cellular proteins by proteolysis within the ubiquitin-proteasome pathway and are presented on the cell surface by MHC class I molecules. Here, we present the crystallographic analysis of yeast 20S proteasome in complex with the inhibitor homobelactosin C. The structure reveals a unique inhibitor-binding mode and provides information about the composition of proteasomal primed substrate-binding sites. IFN-gamma inducible substitution of proteasomal constitutive subunits by immunosubunits modulates characteristics of generated peptides, thus producing fragments with higher preference for binding to MHC class I molecules. The structural data for the proteasome:homobelactosin C complex provide an explanation for involvement of immunosubunits in antigen generation and open perspectives for rational design of ligands, inhibiting exclusively constitutive proteasomes or immunoproteasomes. | lld:pubmed |
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| pubmed-article:16537370 | pubmed:language | eng | lld:pubmed |
| pubmed-article:16537370 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16537370 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:16537370 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:16537370 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:16537370 | pubmed:month | Mar | lld:pubmed |
| pubmed-article:16537370 | pubmed:issn | 0027-8424 | lld:pubmed |
| pubmed-article:16537370 | pubmed:author | pubmed-author:HuberRobertR | lld:pubmed |
| pubmed-article:16537370 | pubmed:author | pubmed-author:de... | lld:pubmed |
| pubmed-article:16537370 | pubmed:author | pubmed-author:GrollMichaelM | lld:pubmed |
| pubmed-article:16537370 | pubmed:author | pubmed-author:LarionovOleg... | lld:pubmed |
| pubmed-article:16537370 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:16537370 | pubmed:day | 21 | lld:pubmed |
| pubmed-article:16537370 | pubmed:volume | 103 | lld:pubmed |
| pubmed-article:16537370 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:16537370 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:16537370 | pubmed:pagination | 4576-9 | lld:pubmed |
| pubmed-article:16537370 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
| pubmed-article:16537370 | pubmed:meshHeading | pubmed-meshheading:16537370... | lld:pubmed |
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| pubmed-article:16537370 | pubmed:meshHeading | pubmed-meshheading:16537370... | lld:pubmed |
| pubmed-article:16537370 | pubmed:meshHeading | pubmed-meshheading:16537370... | lld:pubmed |
| pubmed-article:16537370 | pubmed:meshHeading | pubmed-meshheading:16537370... | lld:pubmed |
| pubmed-article:16537370 | pubmed:meshHeading | pubmed-meshheading:16537370... | lld:pubmed |
| pubmed-article:16537370 | pubmed:meshHeading | pubmed-meshheading:16537370... | lld:pubmed |
| pubmed-article:16537370 | pubmed:meshHeading | pubmed-meshheading:16537370... | lld:pubmed |
| pubmed-article:16537370 | pubmed:meshHeading | pubmed-meshheading:16537370... | lld:pubmed |
| pubmed-article:16537370 | pubmed:year | 2006 | lld:pubmed |
| pubmed-article:16537370 | pubmed:articleTitle | Inhibitor-binding mode of homobelactosin C to proteasomes: new insights into class I MHC ligand generation. | lld:pubmed |
| pubmed-article:16537370 | pubmed:affiliation | Ludwig Maximilians Universität, Adolf Butenandt Institut, Butenandtstrasse 5, Gebäude B, D-81377 Munich, Germany. mgroll@med.uni-muenchen.de | lld:pubmed |
| pubmed-article:16537370 | pubmed:publicationType | Journal Article | lld:pubmed |
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