Comparison of Calpains from Rabbit, Monkey, Human and Rat
Author:
Publisher
Walter de Gruyter GmbH
Subject
Clinical Biochemistry,Molecular Biology,Biochemistry
Link
https://www.degruyter.com/document/doi/10.1515/bchm.1998.379.2.201/pdf
Reference11 articles.
1. Isolation and sequence analyses of cDNA clones for the large subunits of two isozymes of rabbit calcium-dependent protease.
2. A dot-immunobinding assay for monoclonal and other antibodies
3. Preferential localization of calcium-activated neutral protease in epithelial tissues
4. The Amino-Terminal Hydrophobic Region of the Small Subunit of Calcium-Activated Neutral Protease (CANP) Is Essential for Its Activation by Phosphatidylinositol1
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. Calpain activation contributes to oxidative stress-induced pancreatic acinar cell injury;Biochemical Pharmacology;2005-10
2. Dysregulation of the calpain-calpastatin system plays a role in the development of cerulein-induced acute pancreatitis in the rat;American Journal of Physiology-Gastrointestinal and Liver Physiology;2004-06
3. Different expression patterns for ubiquitous calpains and Capn3 splice variants in monkey ocular tissues;Biochimica et Biophysica Acta (BBA) - Gene Structure and Expression;2001-05
4. Calpain as one of the calcium signal mediators in the cell;Neurophysiology;2000-03
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