AH/PH domain-mediated interaction between Akt molecules and its potential role in Akt regulation.

Datta, K; Franke, T F; Chan, T O; Makris, A; Yang, S I; Kaplan, D R; Morrison, D K; Golemis, E A; Tsichlis, P N

Datta, K; Franke, T F; Chan, T O; Makris, A; Yang, S I; Kaplan, D R; Morrison, D K; Golemis, E A; Tsichlis, P N.

Affiliation

Datta K; Fox Chase Cancer Center, Philadelphia, Pennsylvania 19111.

Mol Cell Biol ; 15(4): 2304-10, 1995 Apr.

Article in En | MEDLINE | ID: mdl-7891724

Subject(s)

Protein Serine-Threonine Kinases/metabolism; Proto-Oncogene Proteins/metabolism; Amino Acid Sequence; Animals; Cells, Cultured; Enzyme Activation; Molecular Sequence Data; Mutation; Protein Binding; Protein Serine-Threonine Kinases/genetics; Proto-Oncogene Proteins/genetics; Proto-Oncogene Proteins c-akt; Recombinant Proteins/metabolism; Saccharomyces cerevisiae/genetics; Structure-Activity Relationship

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Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Proto-Oncogene Proteins / Protein Serine-Threonine Kinases Limits: Animals Language: En Journal: Mol Cell Biol Year: 1995 Type: Article

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