CDK-dependent Hsp70 Phosphorylation controls G1 cyclin abundance and cell-cycle progression.

Truman, Andrew W; Kristjansdottir, Kolbrun; Wolfgeher, Donald; Hasin, Naushaba; Polier, Sigrun; Zhang, Hong; Perrett, Sarah; Prodromou, Chrisostomos; Jones, Gary W; Kron, Stephen J

Truman, Andrew W; Kristjansdottir, Kolbrun; Wolfgeher, Donald; Hasin, Naushaba; Polier, Sigrun; Zhang, Hong; Perrett, Sarah; Prodromou, Chrisostomos; Jones, Gary W; Kron, Stephen J.

Affiliation

Truman AW; Ludwig Center for Metastasis Research, The University of Chicago, Chicago, IL 60637, USA.

Cell ; 151(6): 1308-18, 2012 Dec 07.

Article in En | MEDLINE | ID: mdl-23217712

Subject(s)

Adenosine Triphosphatases/metabolism; Cyclins/metabolism; HSP70 Heat-Shock Proteins/metabolism; Saccharomyces cerevisiae Proteins/metabolism; Saccharomyces cerevisiae/metabolism; Cell Cycle; Cell Proliferation; Cyclin D1/metabolism; HEK293 Cells; HSC70 Heat-Shock Proteins/metabolism; Humans; Phosphorylation; Saccharomyces cerevisiae/cytology

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Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Saccharomyces cerevisiae / Cyclins / Adenosine Triphosphatases / HSP70 Heat-Shock Proteins / Saccharomyces cerevisiae Proteins Limits: Humans Language: En Journal: Cell Year: 2012 Type: Article Affiliation country: United States

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