Generation of a subunit III-like protein by autolysis of human and porcine proproteinase E in a binary complex with procarboxypeptidase A
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry,Biophysics
Reference26 articles.
1. The Subunit Structure of Bovine Procarboxypeptidase A-S6.* Chemical Properties and Enzymatic Activities of the Products of Molecular Disaggregation
2. Existence of ternary complexes of procarboxypeptidase A in the pancreas of some ruminant species
3. Further studies on subunit III of bovine procarboxypeptidase A
4. Two-step dissociation of bovine 6S procarboxypeptidase A by dimethylmaleylation
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1. Complex Formation of Human Proelastases with Procarboxypeptidases A1 and A2;Journal of Biological Chemistry;2016-08
2. Cutting at the right place. The importance of selective limited proteolysis in the activation of proproteinase E;European Journal of Biochemistry;1998-02
3. Crystal structure of an oligomer of proteolytic zymogens: detailed conformational analysis of the bovine ternary complex and implications for their activation 1 1Edited by I. A. Wilson;Journal of Molecular Biology;1997-07
4. Crystallization and preliminary X-ray analysis of the ternary complex of procarboxypeptidase A from bovine pancreas;FEBS Letters;1995-07-03
5. Procarboxypeptidase in rat pancreas Overall characterization and comparison of the activation processes;European Journal of Biochemistry;1994-05
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