Data comparing the kinetics of procollagen type I processing by bone morphogenetic protein 1 (BMP-1) with and without procollagen C-proteinase enhancer 1 (PCPE-1)
Author:
Funder
Israel Science Foundation (EK)
Publisher
Elsevier BV
Subject
Multidisciplinary
Reference5 articles.
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2. Substrate-specific modulation of a multisubstrate proteinase. C-terminal processing of fibrillar procollagens is the only BMP-1-dependent activity to be enhanced by PCPE-1;Moali;J. Biol. Chem.,2005
3. Binding of procollagen C-proteinase enhancer-1 (PCPE-1) to heparin/heparan sulfate. Properties and role in PCPE-1 interaction with cells;Weiss;J. Biol. Chem.,2010
4. Bone morphogenetic protein-1: the type I procollagen C-proteinase;Kessler;Science,1996
5. A method for assaying the activity of the endopeptidase which excises the nonhelical carboxyterminal extensions from type I procollagen;Kessler;Anal. Biochem.,1978
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1. Using a peptide-based mass spectrometry approach to quantitate proteolysis of an intact heterogeneous procollagen substrate by BMP1 for antagonistic antibody screening;Analytical and Bioanalytical Chemistry;2022-07-12
2. Procollagen C-proteinase enhancer-1 (PCPE-1), a potential biomarker and therapeutic target for fibrosis;Matrix Biology Plus;2021-08
3. Procollagen C-Proteinase Enhancer 1 (PCPE-1) is a marker of myocardial fibrosis and impaired cardiac function in a murine model of pressure overload;2021-03-07
4. Roles of the procollagen C-propeptides in health and disease;Essays in Biochemistry;2019-06-26
5. Structural Basis for the Acceleration of Procollagen Processing by Procollagen C-Proteinase Enhancer-1;Structure;2018-10
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