| pubmed-article:9096325 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:9096325 | lifeskim:mentions | umls-concept:C0086418 | lld:lifeskim |
| pubmed-article:9096325 | lifeskim:mentions | umls-concept:C0208355 | lld:lifeskim |
| pubmed-article:9096325 | lifeskim:mentions | umls-concept:C0449830 | lld:lifeskim |
| pubmed-article:9096325 | lifeskim:mentions | umls-concept:C1711351 | lld:lifeskim |
| pubmed-article:9096325 | pubmed:issue | 7 | lld:pubmed |
| pubmed-article:9096325 | pubmed:dateCreated | 1997-5-8 | lld:pubmed |
| pubmed-article:9096325 | pubmed:abstractText | In human 20S proteasomes two copies of each of seven different alpha-type and seven different beta-type subunits are assembled to form a stack of four seven-membered rings, giving the general structure alpha(1-7), beta(1-7), beta(1-7), alpha(1-7). By means of immunoelectron microscopy and chemical crosslinking of neighboring subunits, we have determined the positions of the individual subunits in the proteasome. The topography shows that for the trypsin-like, the chymotrypsin-like, and the postglutamyl cleaving activities, the pairs of beta type subunits, which are thought to form active sites, are nearest neighbors. | lld:pubmed |
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| pubmed-article:9096325 | pubmed:language | eng | lld:pubmed |
| pubmed-article:9096325 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9096325 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:9096325 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:9096325 | pubmed:month | Apr | lld:pubmed |
| pubmed-article:9096325 | pubmed:issn | 0027-8424 | lld:pubmed |
| pubmed-article:9096325 | pubmed:author | pubmed-author:HendilK BKB | lld:pubmed |
| pubmed-article:9096325 | pubmed:author | pubmed-author:DahlmannBB | lld:pubmed |
| pubmed-article:9096325 | pubmed:author | pubmed-author:KoppFF | lld:pubmed |
| pubmed-article:9096325 | pubmed:author | pubmed-author:KristensenPP | lld:pubmed |
| pubmed-article:9096325 | pubmed:author | pubmed-author:UerkvitzWW | lld:pubmed |
| pubmed-article:9096325 | pubmed:author | pubmed-author:SobekAA | lld:pubmed |
| pubmed-article:9096325 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:9096325 | pubmed:day | 1 | lld:pubmed |
| pubmed-article:9096325 | pubmed:volume | 94 | lld:pubmed |
| pubmed-article:9096325 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:9096325 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:9096325 | pubmed:pagination | 2939-44 | lld:pubmed |
| pubmed-article:9096325 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
| pubmed-article:9096325 | pubmed:meshHeading | pubmed-meshheading:9096325-... | lld:pubmed |
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| pubmed-article:9096325 | pubmed:meshHeading | pubmed-meshheading:9096325-... | lld:pubmed |
| pubmed-article:9096325 | pubmed:year | 1997 | lld:pubmed |
| pubmed-article:9096325 | pubmed:articleTitle | Subunit arrangement in the human 20S proteasome. | lld:pubmed |
| pubmed-article:9096325 | pubmed:affiliation | Diabetes Forschungsinstitut, Düsseldorf, Germany. | lld:pubmed |
| pubmed-article:9096325 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:9096325 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| entrez-gene:5687 | entrezgene:pubmed | pubmed-article:9096325 | lld:entrezgene |
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