Procaspase-3 and Poly(ADP)ribose Polymerase (PARP) Are Calpain Substrates
- 1 September 1999
- journal article
- Published by Elsevier in Biochemical and Biophysical Research Communications
- Vol. 263 (1) , 94-99
- https://doi.org/10.1006/bbrc.1999.1315
Abstract
No abstract availableKeywords
This publication has 30 references indexed in Scilit:
- Excitotoxins in Neuronal Apoptosis and NecrosisJournal of Cerebral Blood Flow & Metabolism, 1999
- Cleavage of the calpain inhibitor, calpastatin, during apoptosisCell Death & Differentiation, 1998
- Calpain activation is upstream of caspases in radiation-induced apoptosisCell Death & Differentiation, 1998
- Simultaneous Degradation of αII- and βII-Spectrin by Caspase 3 (CPP32) in Apoptotic CellsJournal of Biological Chemistry, 1998
- Calpain: A Protease in Search of a Function?Biochemical and Biophysical Research Communications, 1998
- Caspases: killer proteasesTrends in Biochemical Sciences, 1997
- Isolation and identification of a proteinase from calf thymus that cleaves poly(ADP-ribose) polymerase and histone H1Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1997
- Involvement of Cellular Proteolytic Machinery in ApoptosisBiochemical and Biophysical Research Communications, 1997
- Different Cleavage Pattern for Poly(ADP-Ribose) Polymerase during Necrosis and Apoptosis in HL-60 CellsBiochemical and Biophysical Research Communications, 1996
- Phosphorylation of τ In Situ: Inhibition of Calcium‐Dependent ProteolysisJournal of Neurochemistry, 1995