Further studies on the human pancreatic binary complexes involving procarboxypeptidase A
Author:
Publisher
Wiley
Subject
Cell Biology,Genetics,Molecular Biology,Biochemistry,Structural Biology,Biophysics
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1016/0014-5793(90)80665-6/fullpdf
Reference26 articles.
1. Procarboxypeptidase A-S6.* Further Studies of its Isolation and Properties
2. Existence of ternary complexes of procarboxypeptidase A in the pancreas of some ruminant species
3. Mode of activation and N-terminal sequence of subunit II in bovine procarboxypeptidase A and of porcine chymotrypsinogen C
4. The inactive subunit of ruminant procarboxypeptidase A-S6 complexes. Structural basis of inactivity and physiological role
5. Subunit III of ruminant procarboxypeptidase A-S6 complexes and pancreatic proteases E a new family of pancreatic serine endopeptidases?
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1. Novel p.G250A Mutation Associated with Chronic Pancreatitis Highlights Misfolding-Prone Region in Carboxypeptidase A1 (CPA1);International Journal of Molecular Sciences;2022-12-07
2. Protease propeptide structures, mechanisms of activation, and functions;Critical Reviews in Biochemistry and Molecular Biology;2020-03-03
3. Genetic Analysis of Human Chymotrypsin-Like Elastases 3A and 3B (CELA3A and CELA3B) to Assess the Role of Complex Formation between Proelastases and Procarboxypeptidases in Chronic Pancreatitis;International Journal of Molecular Sciences;2016-12-20
4. Complex Formation of Human Proelastases with Procarboxypeptidases A1 and A2;Journal of Biological Chemistry;2016-08
5. The ovine pancreatic protein which binds insulin-like growth factor binding protein-3 is procarboxypeptidase A;Journal of Endocrinology;1996-07
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