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  • 1
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    Requirement of p27Kip1 for restriction point control of the fibroblast cell cycle (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-05-10
    Description: Cells deprived of serum mitogens will either undergo immediate cell cycle arrest or complete mitosis and arrest in the next cell cycle. The transition from mitogen dependence to mitogen independence occurs in the mid-to late G1 phase of the cell cycle and is called the restriction point. Murine Balb/c-3T3 fibroblasts deprived of serum mitogens accumulated the cyclin-dependent kinase (CDK) inhibitor p27Kip1. This was correlated with inactivation of essential G1 cyclin-CDK complexes and with cell cycle arrest in G1. The ability of specific mitogens to allow transit through the restriction point paralleled their ability to down-regulate p27, and antisense inhibition of p27 expression prevented cell cycle arrest in response to mitogen depletion. Therefore, p27 is an essential component of the pathway that connects mitogenic signals to the cell cycle at the restriction point.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Coats, S -- Flanagan, W M -- Nourse, J -- Roberts, J M -- New York, N.Y. -- Science. 1996 May 10;272(5263):877-80.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Basic Sciences, Fred Hutchinson Cancer Research Center, Seattle, WA 98104, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8629023" target="_blank"〉PubMed〈/a〉
    Keywords: 3T3 Cells ; Amino Acid Sequence ; Animals ; Base Sequence ; *Cell Cycle Proteins ; Culture Media ; Cyclin-Dependent Kinase Inhibitor p27 ; Cyclin-Dependent Kinases/*antagonists & inhibitors/metabolism ; Cyclins/metabolism ; Down-Regulation ; Enzyme Inhibitors/*metabolism ; Epidermal Growth Factor/pharmacology ; *G1 Phase ; Gene Expression/drug effects ; Insulin-Like Growth Factor I/pharmacology ; Mice ; Microtubule-Associated Proteins/biosynthesis/genetics/*metabolism ; Mitogens/pharmacology ; Molecular Sequence Data ; Oligonucleotides, Antisense/pharmacology ; Platelet-Derived Growth Factor/pharmacology ; Proto-Oncogene Proteins c-sis ; *Tumor Suppressor Proteins
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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  • 2
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    Negative regulation of G1 in mammalian cells: inhibition of cyclin E-dependent kinase by TGF-beta (1993)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1993-04-23
    Description: Transforming growth factor-beta (TGF-beta) is a naturally occurring growth inhibitory polypeptide that arrests the cell cycle in middle to late G1 phase. Cells treated with TGF-beta contained normal amounts of cyclin E and cyclin-dependent protein kinase 2 (Cdk2) but failed to stably assemble cyclin E-Cdk2 complexes or accumulate cyclin E-associated kinase activity. Moreover, G1 phase extracts from TGF-beta-treated cells did not support activation of endogenous cyclin-dependent protein kinases by exogenous cyclins. These effects of TGF-beta, which correlated with the inhibition of retinoblastoma protein phosphorylation, suggest that mammalian G1 cyclin-dependent kinases, like their counterparts in yeast, are targets for negative regulators of the cell cycle.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Koff, A -- Ohtsuki, M -- Polyak, K -- Roberts, J M -- Massague, J -- New York, N.Y. -- Science. 1993 Apr 23;260(5107):536-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Basic Sciences, Fred Hutchinson Cancer Research Center, Seattle, WA 98104.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8475385" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *CDC2-CDC28 Kinases ; Cell Extracts ; Cell Line ; Cyclin-Dependent Kinase 2 ; *Cyclin-Dependent Kinases ; Cyclins/*metabolism/pharmacology ; Enzyme Activation/drug effects ; *G1 Phase ; Mink ; Phosphorylation ; Protein Kinases/*metabolism ; *Protein-Serine-Threonine Kinases ; Retinoblastoma Protein/metabolism ; Transforming Growth Factor beta/*pharmacology
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
    Location Call Number Expected Availability
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    PAPER CURRENT
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