The calpain-calpastatin system: structural and functional properties
- 30 September 1991
- journal article
- review article
- Published by Elsevier in The Journal of Nutritional Biochemistry
- Vol. 2 (9) , 467-476
- https://doi.org/10.1016/0955-2863(91)90102-b
Abstract
No abstract availableThis publication has 53 references indexed in Scilit:
- Identification of an endogenous activator of calpain in rat skeletal muscleBiochemical and Biophysical Research Communications, 1990
- Isovalerylcarnitine is a specific activator of the high calcium requiring calpain formsBiochemical and Biophysical Research Communications, 1990
- Proteolytic modification of calcium-dependent protease 1 in erythrocytes treated with ionomycin and calciumBiochemistry, 1989
- Calcium-activated neutral protease inhibitor from rabbit erythrocytes lacks the N-terminal region of the liver inhibitor but retains three inhibitory unitsBiochemical and Biophysical Research Communications, 1987
- Fusion of rat erythrocytes by membrane-mobility agent A2C depends on membrane proteolysis by a cytoplasmic calpainEuropean Journal of Biochemistry, 1986
- Characterization of the defective calpain-endogenous calpain inhibitor system in erythrocytes from Milan hypertensive ratsBiochemical and Biophysical Research Communications, 1986
- Are Intermediate Filament Proteins Involved in Gene Expression?Annals of the New York Academy of Sciences, 1985
- Following association to the membrane, human erythrocyte procalpain is converted and released as fully active calpainBiochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1985
- Binding to erythrocyte membrane is the physiological mechanism for activation of Ca2+-dependent neutral proteinaseBiochemical and Biophysical Research Communications, 1985
- Proteolysis of the epidermal growth factor receptor by endogenous calcium-activated neutral protease from rat liverBiochemical and Biophysical Research Communications, 1983