pubmed-article:9552364 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:9552364 | lifeskim:mentions | umls-concept:C0178453 | lld:lifeskim |
pubmed-article:9552364 | lifeskim:mentions | umls-concept:C0392209 | lld:lifeskim |
pubmed-article:9552364 | lifeskim:mentions | umls-concept:C0031727 | lld:lifeskim |
pubmed-article:9552364 | lifeskim:mentions | umls-concept:C1332741 | lld:lifeskim |
pubmed-article:9552364 | lifeskim:mentions | umls-concept:C1155872 | lld:lifeskim |
pubmed-article:9552364 | lifeskim:mentions | umls-concept:C1704666 | lld:lifeskim |
pubmed-article:9552364 | lifeskim:mentions | umls-concept:C1517892 | lld:lifeskim |
pubmed-article:9552364 | lifeskim:mentions | umls-concept:C0208973 | lld:lifeskim |
pubmed-article:9552364 | pubmed:dateCreated | 1998-4-30 | lld:pubmed |
pubmed-article:9552364 | pubmed:abstractText | Close connections appear to exist between extra-cellular signals that regulate cell proliferation and the protein kinases that control the cell cycle machinery. The fission yeast nim1 kinase is an inducer of cdc2 kinase activity acting through the inhibition of wee1 kinase. Nim1 function is required for a correct cellular response to nutritional starvation. In the absence of nim1, starved cells are unable to decrease their size at mitosis, to arrest their cycle in G1 and to enter G0. Here, we review our current knowledge on the role and the regulation of nim1 in connecting cell cycle and nutritional pathways. | lld:pubmed |
pubmed-article:9552364 | pubmed:language | eng | lld:pubmed |
pubmed-article:9552364 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:9552364 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:9552364 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:9552364 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:9552364 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:9552364 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:9552364 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:9552364 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:9552364 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:9552364 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:9552364 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:9552364 | pubmed:issn | 1087-2957 | lld:pubmed |
pubmed-article:9552364 | pubmed:author | pubmed-author:OustrinM LML | lld:pubmed |
pubmed-article:9552364 | pubmed:author | pubmed-author:BelenguerPP | lld:pubmed |
pubmed-article:9552364 | pubmed:author | pubmed-author:DucommunBB | lld:pubmed |
pubmed-article:9552364 | pubmed:author | pubmed-author:BaldinVV | lld:pubmed |
pubmed-article:9552364 | pubmed:author | pubmed-author:PelloquinLL | lld:pubmed |
pubmed-article:9552364 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:9552364 | pubmed:volume | 1 | lld:pubmed |
pubmed-article:9552364 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:9552364 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:9552364 | pubmed:pagination | 207-14 | lld:pubmed |
pubmed-article:9552364 | pubmed:dateRevised | 2009-11-19 | lld:pubmed |
pubmed-article:9552364 | pubmed:meshHeading | pubmed-meshheading:9552364-... | lld:pubmed |
pubmed-article:9552364 | pubmed:meshHeading | pubmed-meshheading:9552364-... | lld:pubmed |
pubmed-article:9552364 | pubmed:meshHeading | pubmed-meshheading:9552364-... | lld:pubmed |
pubmed-article:9552364 | pubmed:meshHeading | pubmed-meshheading:9552364-... | lld:pubmed |
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pubmed-article:9552364 | pubmed:meshHeading | pubmed-meshheading:9552364-... | lld:pubmed |
pubmed-article:9552364 | pubmed:meshHeading | pubmed-meshheading:9552364-... | lld:pubmed |
pubmed-article:9552364 | pubmed:meshHeading | pubmed-meshheading:9552364-... | lld:pubmed |
pubmed-article:9552364 | pubmed:meshHeading | pubmed-meshheading:9552364-... | lld:pubmed |
pubmed-article:9552364 | pubmed:year | 1995 | lld:pubmed |
pubmed-article:9552364 | pubmed:articleTitle | The fission yeast Nim1/Cdr1 kinase: a link between nutritional state and cell cycle control. | lld:pubmed |
pubmed-article:9552364 | pubmed:affiliation | Laboratoire de Pharmacologie et de Toxicologie Fondamentales, CNRS, Université Paul Sabatier, Toulouse, France. | lld:pubmed |
pubmed-article:9552364 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:9552364 | pubmed:publicationType | Review | lld:pubmed |
pubmed-article:9552364 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |