Structure–Function Analysis of the 7B2 CT Peptide
- 27 January 2000
- journal article
- Published by Elsevier in Biochemical and Biophysical Research Communications
- Vol. 267 (3) , 940-942
- https://doi.org/10.1006/bbrc.1999.2060
Abstract
No abstract availableKeywords
This publication has 12 references indexed in Scilit:
- Proteolytic Processing in the Secretory PathwayJournal of Biological Chemistry, 1999
- Solution Structure of a Retro-inverso Peptide Analogue Mimicking the Foot-and-Mouth Disease Virus Major Antigenic SiteJournal of Biological Chemistry, 1999
- The Proteolytic Maturation of Prohormone Convertase 2 (PC2) is a pH-Driven ProcessArchives of Biochemistry and Biophysics, 1999
- The Cell Biology of the Prohormone Convertases PCI and PC2Published by Elsevier ,1999
- Structural comparison between retro-inverso and parent peptides: Molecular basis for the biological activity of a retro-inverso analogue of the immunodominant fragment of VP1 coat protein from foot-and-mouth disease virusBiopolymers, 1997
- Internal cleavage of the inhibitory 7B2 carboxyl-terminal peptide by PC2: a potential mechanism for its inactivation.Proceedings of the National Academy of Sciences, 1996
- Inhibition of angiotensin converting enzyme and potentiation of bradykinin by retro-inverso analogues of short peptides and sequences related to angiotensin I and bradykininBiochemical Pharmacology, 1996
- Identification of the Region within the Neuroendocrine Polypeptide 7B2 Responsible for the Inhibition of Prohormone Convertase PC2Published by Elsevier ,1995
- Enzymic characterization of immunopurified prohormone convertase 2: Potent inhibition by a 7B2 peptide fragmentBiochemistry, 1995
- The neuroendocrine polypeptide 7B2 is an endogenous inhibitor of prohormone convertase PC2.Proceedings of the National Academy of Sciences, 1994