pubmed-article:7954792 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:7954792 | lifeskim:mentions | umls-concept:C0036025 | lld:lifeskim |
pubmed-article:7954792 | lifeskim:mentions | umls-concept:C0919418 | lld:lifeskim |
pubmed-article:7954792 | lifeskim:mentions | umls-concept:C1705165 | lld:lifeskim |
pubmed-article:7954792 | lifeskim:mentions | umls-concept:C2587213 | lld:lifeskim |
pubmed-article:7954792 | lifeskim:mentions | umls-concept:C2700061 | lld:lifeskim |
pubmed-article:7954792 | pubmed:issue | 2 | lld:pubmed |
pubmed-article:7954792 | pubmed:dateCreated | 1994-11-29 | lld:pubmed |
pubmed-article:7954792 | pubmed:abstractText | When yeast cells reach a critical size, they initiate bud formation, spindle pole body duplication, and DNA replication almost simultaneously. All three events depend on activation of Cdc28 protein kinase by the G1 cyclins Cln1, -2, and -3. We show that DNA replication also requires activation of Cdc28 by B-type (Clb) cyclins. A sextuple clb1-6 mutant arrests as multibudded G1 cells that resemble cells lacking the Cdc34 ubiquitin-conjugating enzyme. cdc34 mutants cannot enter S phase because they fail to destroy p40SIC1, which is a potent inhibitor of Clb but not Cln forms of the Cdc28 kinase. In wild-type cells, p40SIC1 protein appears at the end of mitosis and disappears shortly before S phase. Proteolysis of a cyclin-specific inhibitor of Cdc28 is therefore an essential aspect of the G1 to S phase transition. | lld:pubmed |
pubmed-article:7954792 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:7954792 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:7954792 | pubmed:language | eng | lld:pubmed |
pubmed-article:7954792 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:7954792 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:7954792 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:7954792 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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pubmed-article:7954792 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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pubmed-article:7954792 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:7954792 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:7954792 | pubmed:month | Oct | lld:pubmed |
pubmed-article:7954792 | pubmed:issn | 0092-8674 | lld:pubmed |
pubmed-article:7954792 | pubmed:author | pubmed-author:NasmythKK | lld:pubmed |
pubmed-article:7954792 | pubmed:author | pubmed-author:BöhmTT | lld:pubmed |
pubmed-article:7954792 | pubmed:author | pubmed-author:SchwobEE | lld:pubmed |
pubmed-article:7954792 | pubmed:author | pubmed-author:MendenhallM... | lld:pubmed |
pubmed-article:7954792 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:7954792 | pubmed:day | 21 | lld:pubmed |
pubmed-article:7954792 | pubmed:volume | 79 | lld:pubmed |
pubmed-article:7954792 | pubmed:geneSymbol | CDC28 | lld:pubmed |
pubmed-article:7954792 | pubmed:geneSymbol | SIC1 | lld:pubmed |
pubmed-article:7954792 | pubmed:geneSymbol | CLB2 | lld:pubmed |
pubmed-article:7954792 | pubmed:geneSymbol | CLB4 | lld:pubmed |
pubmed-article:7954792 | pubmed:geneSymbol | CLB3 | lld:pubmed |
pubmed-article:7954792 | pubmed:geneSymbol | CLB1 | lld:pubmed |
pubmed-article:7954792 | pubmed:geneSymbol | CLB6 | lld:pubmed |
pubmed-article:7954792 | pubmed:geneSymbol | CLB5 | lld:pubmed |
pubmed-article:7954792 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:7954792 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:7954792 | pubmed:pagination | 233-44 | lld:pubmed |
pubmed-article:7954792 | pubmed:dateRevised | 2009-11-19 | lld:pubmed |
pubmed-article:7954792 | pubmed:meshHeading | pubmed-meshheading:7954792-... | lld:pubmed |
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pubmed-article:7954792 | pubmed:meshHeading | pubmed-meshheading:7954792-... | lld:pubmed |
pubmed-article:7954792 | pubmed:year | 1994 | lld:pubmed |
pubmed-article:7954792 | pubmed:articleTitle | The B-type cyclin kinase inhibitor p40SIC1 controls the G1 to S transition in S. cerevisiae. | lld:pubmed |
pubmed-article:7954792 | pubmed:affiliation | I. M. P. Research Institute of Molecular Pathology, Vienna, Austria. | lld:pubmed |
pubmed-article:7954792 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:7954792 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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