- Caspase 3
Caspase 3 is a
caspase protein. It interacts withcaspase 8 .PBB_Summary
section_title =
summary_text = This gene encodes a protein that is a member of the cysteine-aspartic acid protease (caspase) family. Sequential activation of caspases plays a central role in the execution-phase of cell apoptosis. Caspases exist as inactive proenzymes that undergo proteolytic processing at conserved aspartic residues to produce two subunits, large and small, that dimerize to form the active enzyme. This protein cleaves and activates caspases 6, 7, and 9; and the protein itself is processed by caspases 8, 9, and 10. It is the predominant caspase involved in the cleavage of amyloid-beta 4A precursor protein, which is associated with neuronal death in Alzheimer's disease. Alternative splicing of this gene results in two transcript variants that encode the same protein. [cite web | title = Entrez Gene: CASP3 caspase 3, apoptosis-related cysteine peptidase| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=836| accessdate = ]References
Further reading
PBB_Further_reading
citations =
*cite journal | author=Cohen GM |title=Caspases: the executioners of apoptosis. |journal=Biochem. J. |volume=326 ( Pt 1) |issue= |pages= 1–16 |year= 1997 |pmid= 9337844 |doi=
*cite journal | author=Roig J, Traugh JA |title=Cytostatic p21 G protein-activated protein kinase gamma-PAK. |journal=Vitam. Horm. |volume=62 |issue= |pages= 167–98 |year= 2001 |pmid= 11345898 |doi=
*cite journal | author=Zhao LJ, Zhu H |title=Structure and function of HIV-1 auxiliary regulatory protein Vpr: novel clues to drug design. |journal=Curr. Drug Targets Immune Endocr. Metabol. Disord. |volume=4 |issue= 4 |pages= 265–75 |year= 2005 |pmid= 15578977 |doi=
*cite journal | author=Le Rouzic E, Benichou S |title=The Vpr protein from HIV-1: distinct roles along the viral life cycle. |journal=Retrovirology |volume=2 |issue= |pages= 11 |year= 2006 |pmid= 15725353 |doi= 10.1186/1742-4690-2-11
*cite journal | author=Sykes MC, Mowbray AL, Jo H |title=Reversible glutathiolation of caspase-3 by glutaredoxin as a novel redox signaling mechanism in tumor necrosis factor-alpha-induced cell death. |journal=Circ. Res. |volume=100 |issue= 2 |pages= 152–4 |year= 2007 |pmid= 17272816 |doi= 10.1161/01.RES.0000258171.08020.72PBB_Controls
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