| pubmed-article:7624798 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:7624798 | lifeskim:mentions | umls-concept:C0035820 | lld:lifeskim |
| pubmed-article:7624798 | lifeskim:mentions | umls-concept:C0169665 | lld:lifeskim |
| pubmed-article:7624798 | lifeskim:mentions | umls-concept:C1704259 | lld:lifeskim |
| pubmed-article:7624798 | lifeskim:mentions | umls-concept:C1705987 | lld:lifeskim |
| pubmed-article:7624798 | lifeskim:mentions | umls-concept:C2346714 | lld:lifeskim |
| pubmed-article:7624798 | lifeskim:mentions | umls-concept:C1998811 | lld:lifeskim |
| pubmed-article:7624798 | pubmed:issue | 5224 | lld:pubmed |
| pubmed-article:7624798 | pubmed:dateCreated | 1995-8-31 | lld:pubmed |
| pubmed-article:7624798 | pubmed:abstractText | The p27 mammalian cell cycle protein is an inhibitor of cyclin-dependent kinases. Both in vivo and in vitro, p27 was found to be degraded by the ubiquitin-proteasome pathway. The human ubiquitin-conjugating enzymes Ubc2 and Ubc3 were specifically involved in the ubiquitination of p27. Compared with proliferating cells, quiescent cells exhibited a smaller amount of p27 ubiquitinating activity, which accounted for the marked increase of p27 half-life measured in these cells. Thus, the abundance of p27 in cells is regulated by degradation. The specific proteolysis of p27 may represent a mechanism for regulating the activity of cyclin-dependent kinases. | lld:pubmed |
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| pubmed-article:7624798 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:7624798 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:7624798 | pubmed:month | Aug | lld:pubmed |
| pubmed-article:7624798 | pubmed:issn | 0036-8075 | lld:pubmed |
| pubmed-article:7624798 | pubmed:author | pubmed-author:PaganiGG | lld:pubmed |
| pubmed-article:7624798 | pubmed:author | pubmed-author:RolffLL | lld:pubmed |
| pubmed-article:7624798 | pubmed:author | pubmed-author:TamS WSW | lld:pubmed |
| pubmed-article:7624798 | pubmed:author | pubmed-author:ChauVV | lld:pubmed |
| pubmed-article:7624798 | pubmed:author | pubmed-author:Beer-RomeroPP | lld:pubmed |
| pubmed-article:7624798 | pubmed:author | pubmed-author:Del SalGG | lld:pubmed |
| pubmed-article:7624798 | pubmed:author | pubmed-author:YewP RPR | lld:pubmed |
| pubmed-article:7624798 | pubmed:author | pubmed-author:DraettaG FGF | lld:pubmed |
| pubmed-article:7624798 | pubmed:author | pubmed-author:TheodorasA... | lld:pubmed |
| pubmed-article:7624798 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:7624798 | pubmed:day | 4 | lld:pubmed |
| pubmed-article:7624798 | pubmed:volume | 269 | lld:pubmed |
| pubmed-article:7624798 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:7624798 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:7624798 | pubmed:pagination | 682-5 | lld:pubmed |
| pubmed-article:7624798 | pubmed:dateRevised | 2009-11-19 | lld:pubmed |
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| pubmed-article:7624798 | pubmed:year | 1995 | lld:pubmed |
| pubmed-article:7624798 | pubmed:articleTitle | Role of the ubiquitin-proteasome pathway in regulating abundance of the cyclin-dependent kinase inhibitor p27. | lld:pubmed |
| pubmed-article:7624798 | pubmed:affiliation | Mitotix Inc., Cambridge, MA 02139, USA. | lld:pubmed |
| pubmed-article:7624798 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:7624798 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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