Irreversible inactivation of calcium-dependent proteinases from rat liver by biological disulfides
Author:
Publisher
Wiley
Subject
Cell Biology,Genetics,Molecular Biology,Biochemistry,Structural Biology,Biophysics
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1016/0014-5793(87)81302-9/fullpdf
Reference19 articles.
1. Calcium-dependent proteolytic activity in rat liver: Identification of two proteases with different calcium requirements
2. Purification and characterization of calcium-dependent proteases from rat heart.
3. A Ca2+ion-activated protease possibly involved in myofibrillar protein turnover. Purification from porcine muscle
4. Cytosolic calcium dependent proteinase of human erythrocytes: Formation of an enzyme-natural inhibitor complex induced by Ca2+ ions
5. Comparison of Low and High Calcium Requiring Forms of the Calcium-Activated Neutral Protease (CANP) from Rabbit Skeletal Muscle1
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1. The synchronous and reciprocal regulation of the activities of cysteine proteases associated with long-term plasticity;Neurochemical Journal;2013-03
2. Oxidation of Cys278 of ADH I isozyme from Kluyveromyces lactis by naturally occurring disulfides causes its reversible inactivation;Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics;2009-03
3. Cyclosporin A prevents calpain activation despite increased intracellular calcium concentrations, as well as translocation of apoptosis-inducing factor, cytochrome c and caspase-3 activation in neurons exposed to transient hypoglycemia;Journal of Neurochemistry;2003-05-13
4. Inhibition of rat PC12 cell calpain activity by glutathione, oxidized glutathione and nitric oxide;Neuroscience Letters;2001-09
5. Cysteine Proteases and Their Inhibitors;Chemical Reviews;1997-02-01
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