| pubmed-article:1833185 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:1833185 | lifeskim:mentions | umls-concept:C0031715 | lld:lifeskim |
| pubmed-article:1833185 | lifeskim:mentions | umls-concept:C0079183 | lld:lifeskim |
| pubmed-article:1833185 | lifeskim:mentions | umls-concept:C1704675 | lld:lifeskim |
| pubmed-article:1833185 | lifeskim:mentions | umls-concept:C1332721 | lld:lifeskim |
| pubmed-article:1833185 | lifeskim:mentions | umls-concept:C1546857 | lld:lifeskim |
| pubmed-article:1833185 | lifeskim:mentions | umls-concept:C1556066 | lld:lifeskim |
| pubmed-article:1833185 | lifeskim:mentions | umls-concept:C1619636 | lld:lifeskim |
| pubmed-article:1833185 | lifeskim:mentions | umls-concept:C1514873 | lld:lifeskim |
| pubmed-article:1833185 | pubmed:issue | 11 | lld:pubmed |
| pubmed-article:1833185 | pubmed:dateCreated | 1991-11-18 | lld:pubmed |
| pubmed-article:1833185 | pubmed:abstractText | Activation of the cdc2 protein kinase at different stages of the cell cycle is regulated by post-translational modifications and interactions with cyclins. We show that in vitro translated human cdc2 binds very poorly to A and B cyclins, unless it has been preincubated with a Xenopus egg extract. This results in the phosphorylation of cdc2 which allows binding to cyclins. The replacement of Thr161, a residue conserved and phosphorylated in other protein kinases, with valine inhibits cdc2 association with A and B cyclins. In addition, mutations in the amino-terminus of cdc2 and within the conserved 'PSTAIR' region strongly inhibit binding. The Thr161Val mutation causes a lethal phenotype in the fission yeast Schizosaccharomyces pombe, while replacement of Thr161 with glutamic acid, potentially mimicking phosphorylation, causes uncoordination of mitosis and multiple cytokinesis. These results suggest that a threonine phosphorylation/dephosphorylation cycle is involved in regulating cdc2 function. | lld:pubmed |
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| pubmed-article:1833185 | pubmed:language | eng | lld:pubmed |
| pubmed-article:1833185 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1833185 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:1833185 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:1833185 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:1833185 | pubmed:month | Nov | lld:pubmed |
| pubmed-article:1833185 | pubmed:issn | 0261-4189 | lld:pubmed |
| pubmed-article:1833185 | pubmed:author | pubmed-author:FranzaB RBRJr | lld:pubmed |
| pubmed-article:1833185 | pubmed:author | pubmed-author:KarsentiEE | lld:pubmed |
| pubmed-article:1833185 | pubmed:author | pubmed-author:BrambillaPP | lld:pubmed |
| pubmed-article:1833185 | pubmed:author | pubmed-author:DraettaGG | lld:pubmed |
| pubmed-article:1833185 | pubmed:author | pubmed-author:FélixM AMA | lld:pubmed |
| pubmed-article:1833185 | pubmed:author | pubmed-author:DucommunBB | lld:pubmed |
| pubmed-article:1833185 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:1833185 | pubmed:volume | 10 | lld:pubmed |
| pubmed-article:1833185 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:1833185 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:1833185 | pubmed:pagination | 3311-9 | lld:pubmed |
| pubmed-article:1833185 | pubmed:dateRevised | 2009-11-19 | lld:pubmed |
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