pubmed-article:1647011 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:1647011 | lifeskim:mentions | umls-concept:C0041538 | lld:lifeskim |
pubmed-article:1647011 | lifeskim:mentions | umls-concept:C0040649 | lld:lifeskim |
pubmed-article:1647011 | lifeskim:mentions | umls-concept:C1412111 | lld:lifeskim |
pubmed-article:1647011 | lifeskim:mentions | umls-concept:C1417038 | lld:lifeskim |
pubmed-article:1647011 | lifeskim:mentions | umls-concept:C1979845 | lld:lifeskim |
pubmed-article:1647011 | lifeskim:mentions | umls-concept:C1151970 | lld:lifeskim |
pubmed-article:1647011 | lifeskim:mentions | umls-concept:C1704735 | lld:lifeskim |
pubmed-article:1647011 | lifeskim:mentions | umls-concept:C1515655 | lld:lifeskim |
pubmed-article:1647011 | pubmed:issue | 11 | lld:pubmed |
pubmed-article:1647011 | pubmed:dateCreated | 1991-7-19 | lld:pubmed |
pubmed-article:1647011 | pubmed:abstractText | The substrates of ubiquitin-dependent proteolytic pathways include both damaged or otherwise abnormal proteins and undamaged proteins that are naturally short-lived. Few specific examples of the latter class have been identified, however. Previous work has shown that the cell type-specific MAT alpha 2 repressor of the yeast Saccharomyces cerevisiae is an extremely short-lived protein. We now demonstrate that alpha 2 is conjugated to ubiquitin in vivo. More than one lysine residue of alpha 2 can be joined to ubiquitin, and some of the ubiquitin moieties form a Lys48-linked multiubiquitin chain. Overexpression of degradation-impaired ubiquitin variants was used to show that at least a significant fraction of alpha 2 degradation is dependent on its ubiquitination. | lld:pubmed |
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pubmed-article:1647011 | pubmed:language | eng | lld:pubmed |
pubmed-article:1647011 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:1647011 | pubmed:citationSubset | IM | lld:pubmed |
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pubmed-article:1647011 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:1647011 | pubmed:month | Jun | lld:pubmed |
pubmed-article:1647011 | pubmed:issn | 0027-8424 | lld:pubmed |
pubmed-article:1647011 | pubmed:author | pubmed-author:VarshavskyAA | lld:pubmed |
pubmed-article:1647011 | pubmed:author | pubmed-author:HochstrasserM... | lld:pubmed |
pubmed-article:1647011 | pubmed:author | pubmed-author:ChauVV | lld:pubmed |
pubmed-article:1647011 | pubmed:author | pubmed-author:EllisonM JMJ | lld:pubmed |
pubmed-article:1647011 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:1647011 | pubmed:day | 1 | lld:pubmed |
pubmed-article:1647011 | pubmed:volume | 88 | lld:pubmed |
pubmed-article:1647011 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:1647011 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:1647011 | pubmed:pagination | 4606-10 | lld:pubmed |
pubmed-article:1647011 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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pubmed-article:1647011 | pubmed:meshHeading | pubmed-meshheading:1647011-... | lld:pubmed |
pubmed-article:1647011 | pubmed:year | 1991 | lld:pubmed |
pubmed-article:1647011 | pubmed:articleTitle | The short-lived MAT alpha 2 transcriptional regulator is ubiquitinated in vivo. | lld:pubmed |
pubmed-article:1647011 | pubmed:affiliation | Department of Biochemistry and Molecular Biology, University of Chicago, IL 60637. | lld:pubmed |
pubmed-article:1647011 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:1647011 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
pubmed-article:1647011 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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