Role of the COOH-terminal Domains of Meprin A in Folding, Secretion, and Activity of the Metalloendopeptidase
Open Access
- 1 December 1998
- journal article
- Published by Elsevier
- Vol. 273 (52) , 35260-35267
- https://doi.org/10.1074/jbc.273.52.35260
Abstract
No abstract availableKeywords
This publication has 28 references indexed in Scilit:
- Maturation of Secreted Meprin α during Biosynthesis: Role of the Furin Site and Identification of the COOH-Terminal Amino Acids of the Mouse Kidney Metalloprotease SubunitArchives of Biochemistry and Biophysics, 1998
- Cytosolic Degradation of T-cell Receptor α Chains by the ProteasomeJournal of Biological Chemistry, 1997
- Unveiling the Substrate Specificity of Meprin β on the Basis of the Site in Protein Kinase A Cleaved by the Kinase Splitting Membranal ProteinaseJournal of Biological Chemistry, 1997
- Degradation of 3-Hydroxy-3-methylglutaryl-CoA Reductase in Endoplasmic Reticulum Membranes Is Accelerated as a Result of Increased Susceptibility to ProteolysisJournal of Biological Chemistry, 1996
- Cysteine Mutations in the MAM Domain Result in Monomeric Meprin and Alter Stability and Activity of the ProteinasePublished by Elsevier ,1996
- A Novel Meprin β‘ mRNA in Mouse Embryonal and Human Colon Carcinoma CellsPublished by Elsevier ,1996
- The astacin family of metalloendopeptidasesProtein Science, 1995
- The metzincins — Topological and sequential relations between the astacins, adamalysins, serralysins, and matrixins (collagenases) define a super family of zinc‐peptidasesProtein Science, 1995
- Cloning of the PABA peptide hydrolase alpha subunit (PPHα) from human small intestine and its expression in COS‐1 cellsFEBS Letters, 1993
- Maturation of the head of bacteriophage T4Journal of Molecular Biology, 1973