Tyrosine 36 Plays a Critical Role in the Interaction of the AB Loop of Tissue Inhibitor of Metalloproteinases-2 with Matrix Metalloproteinase-14
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry
Reference32 articles.
1. Tissue inhibitors of metalloproteinases: evolution, structure and function
2. Mechanism of inhibition of the human matrix metalloproteinase stromelysin-1 by TIMP-1
3. Crystal structure of the complex formed by the membrane type 1-matrix metalloproteinase with the tissue inhibitor of metalloproteinases-2, the soluble progelatinase A receptor
4. Mapping the Binding Site for Matrix Metalloproteinase on the N-Terminal Domain of the Tissue Inhibitor of Metalloproteinases-2 by NMR Chemical Shift Perturbation
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1. Utilizing genetic code expansion to modify N-TIMP2 specificity towards MMP-2, MMP-9, and MMP-14;Scientific Reports;2023-03-30
2. Metalloproteinases and Their Inhibitors: Potential for the Development of New Therapeutics;Cells;2020-05-25
3. Directed evolution of the metalloproteinase inhibitor TIMP-1 reveals that its N- and C-terminal domains cooperate in matrix metalloproteinase recognition;Journal of Biological Chemistry;2019-06
4. Extracellular Phosphorylation of TIMP-2 by Secreted c-Src Tyrosine Kinase Controls MMP-2 Activity;iScience;2018-03
5. Therapeutic Potential of Matrix Metalloproteinase Inhibition in Breast Cancer;Journal of Cellular Biochemistry;2017-07-17
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