A novel form of DAP5 protein accumulates in apoptotic cells as a result of caspase cleavage and internal ribosome entry site-mediated translation.

Henis-Korenblit, S; Strumpf, N L; Goldstaub, D; Kimchi, A

Henis-Korenblit, S; Strumpf, N L; Goldstaub, D; Kimchi, A.

Affiliation

Henis-Korenblit S; Department of Molecular Genetics, Weizmann Institute of Science, Rehovot 76100, Israel.

Mol Cell Biol ; 20(2): 496-506, 2000 Jan.

Article in En | MEDLINE | ID: mdl-10611228

Subject(s)

Apoptosis; Caspases/metabolism; Eukaryotic Initiation Factor-4G; Protein Biosynthesis/genetics; Proteins/chemistry; Proteins/metabolism; Ribosomes/metabolism; 5' Untranslated Regions/genetics; Animals; Eukaryotic Initiation Factor-3; Eukaryotic Initiation Factor-4A; Humans; Mice; Molecular Weight; Peptide Fragments/metabolism; Peptide Initiation Factors/metabolism; Protein Binding; Protein Processing, Post-Translational; Proteins/genetics; RNA Caps/genetics; RNA Caps/physiology; RNA, Messenger/genetics; RNA, Messenger/physiology; Tumor Cells, Cultured; Tumor Suppressor Protein p53/physiology; Up-Regulation; fas Receptor/physiology

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Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Ribosomes / Protein Biosynthesis / Proteins / Apoptosis / Caspases / Eukaryotic Initiation Factor-4G Type of study: Prognostic_studies Limits: Animals / Humans Language: En Journal: Mol Cell Biol Year: 2000 Type: Article Affiliation country: Israel

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