MMP-12 Catalytic Domain Recognizes Triple Helical Peptide Models of Collagen V with Exosites and High Activity
Open Access
- 1 August 2008
- journal article
- Published by Elsevier
- Vol. 283 (31) , 21779-21788
- https://doi.org/10.1074/jbc.m709966200
Abstract
No abstract availableKeywords
This publication has 92 references indexed in Scilit:
- Solution Structure of Inhibitor-Free Human Metalloelastase (MMP-12) Indicates an Internal Conformational AdjustmentJournal of Molecular Biology, 2007
- Rapid determination of enzyme kinetics from fluorescence: Overcoming the inner filter effectAnalytical Biochemistry, 2007
- MEROPS: the peptidase databaseNucleic Acids Research, 2007
- Differentiation of Secreted and Membrane-Type Matrix Metalloproteinase Activities Based on Substitutions and Interruptions of Triple-Helical SequencesBiochemistry, 2007
- 1H, 13C, and 15N peak assignments and secondary structure of human macrophage metalloelastase (MMP-12) in its inhibitor-free stateJournal of Biomolecular NMR, 2006
- Stabilization of atherosclerotic plaques: New mechanisms and clinical targetsNature Medicine, 2002
- Hydrolysis of Triple-helical Collagen Peptide Models by Matrix MetalloproteinasesPublished by Elsevier ,2000
- SWISS‐MODEL and the Swiss‐Pdb Viewer: An environment for comparative protein modelingElectrophoresis, 1997
- NMRPipe: A multidimensional spectral processing system based on UNIX pipesJournal of Biomolecular NMR, 1995
- Mutation of the Active Site Glutamic Acid of Human Gelatinase A: Effects on Latency, Catalysis, and the Binding of Tissue Inhibitor of Metalloproteinases-1Biochemistry, 1994