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| pubmed-article:10926487 | lifeskim:mentions | umls-concept:C0243126 | lld:lifeskim |
| pubmed-article:10926487 | lifeskim:mentions | umls-concept:C0205396 | lld:lifeskim |
| pubmed-article:10926487 | lifeskim:mentions | umls-concept:C0280024 | lld:lifeskim |
| pubmed-article:10926487 | lifeskim:mentions | umls-concept:C0280075 | lld:lifeskim |
| pubmed-article:10926487 | lifeskim:mentions | umls-concept:C0936012 | lld:lifeskim |
| pubmed-article:10926487 | lifeskim:mentions | umls-concept:C1334043 | lld:lifeskim |
| pubmed-article:10926487 | pubmed:issue | 1 | lld:pubmed |
| pubmed-article:10926487 | pubmed:dateCreated | 2000-9-6 | lld:pubmed |
| pubmed-article:10926487 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10926487 | pubmed:abstractText | Biogenesis of mammalian 20 S proteasomes occurs via precursor complexes containing alpha and unprocessed beta subunits. A human homologue of the yeast proteasome maturation factor Ump1 was identified in 2D gels of 16 S precursor preparations and designated as POMP (proteasome maturation protein). We show that POMP is detected only in precursor fractions and not in fractions containing mature 20 S proteasome. Northern blot experiments revealed that expression of POMP is induced after treatment with interferon gamma. To analyse the role of the beta 5 propeptide for proper maturation and incorporation of the beta 5 subunit into the complex, human T2 cells, which highly express derivatives of the beta 5i subunit (LMP7), were studied. In contrast to yeast, the presence of the beta 5 propeptide is not essential for incorporation of LMP7 into the proteasome complex. Mutated LMP7 subunits either carrying the prosequence of beta 2i (LMP2) or containing a mutation in the active threonine site are incorporated like wild-type LMP7, while a LMP7 derivative lacking the prosequence completely is incorporated to a lesser extent. Although the absence of the prosequence does not affect incorporation of LMP7, its deletion leads to delayed proteasome maturation and thereby to an accumulation of precursor complexes. As a result of the precursor accumulation, an increased amount of the POMP protein can be detected in these cells. | lld:pubmed |
| pubmed-article:10926487 | pubmed:language | eng | lld:pubmed |
| pubmed-article:10926487 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10926487 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:10926487 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:10926487 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:10926487 | pubmed:month | Aug | lld:pubmed |
| pubmed-article:10926487 | pubmed:issn | 0022-2836 | lld:pubmed |
| pubmed-article:10926487 | pubmed:author | pubmed-author:SchmidtMM | lld:pubmed |
| pubmed-article:10926487 | pubmed:author | pubmed-author:WittEE | lld:pubmed |
| pubmed-article:10926487 | pubmed:author | pubmed-author:KraftRR | lld:pubmed |
| pubmed-article:10926487 | pubmed:author | pubmed-author:KrügerEE | lld:pubmed |
| pubmed-article:10926487 | pubmed:author | pubmed-author:KloetzelP MPM | lld:pubmed |
| pubmed-article:10926487 | pubmed:author | pubmed-author:ZantopfDD | lld:pubmed |
| pubmed-article:10926487 | pubmed:copyrightInfo | Copyright 2000 Academic Press. | lld:pubmed |
| pubmed-article:10926487 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:10926487 | pubmed:day | 4 | lld:pubmed |
| pubmed-article:10926487 | pubmed:volume | 301 | lld:pubmed |
| pubmed-article:10926487 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:10926487 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:10926487 | pubmed:pagination | 1-9 | lld:pubmed |
| pubmed-article:10926487 | pubmed:dateRevised | 2008-11-21 | lld:pubmed |
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| pubmed-article:10926487 | pubmed:year | 2000 | lld:pubmed |
| pubmed-article:10926487 | pubmed:articleTitle | Characterisation of the newly identified human Ump1 homologue POMP and analysis of LMP7(beta 5i) incorporation into 20 S proteasomes. | lld:pubmed |
| pubmed-article:10926487 | pubmed:affiliation | Institut für Biochemie, Charité-Humboldt University Medical School, Monbijoustr.2, Berlin, 10117, Germany. | lld:pubmed |
| pubmed-article:10926487 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:10926487 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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