Total Conversion of Tissue Inhibitor of Metalloproteinase (TIMP) for Specific Metalloproteinase Targeting
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry
Reference32 articles.
1. Solution structure of the active domain of tissue inhibitor of metalloproteinases-2. A new member of the OB fold protein family
2. Mechanism of inhibition of the human matrix metalloproteinase stromelysin-1 by TIMP-1
3. Three-dimensional structure of human tissue inhibitor of metalloproteinases-2 at 2.1 Å resolution
4. 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
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1. An integrative analysis reveals the prognostic and immunological role of TIMP gene family in pan-cancer;2023-08-24
2. Unravelling the distinct biological functions and potential therapeutic applications of TIMP2 in cancer;Carcinogenesis;2022-04-18
3. Biology of Tissue Inhibitor of Metalloproteinase 3 (TIMP3), and Its Therapeutic Implications in Cardiovascular Pathology;Frontiers in Physiology;2020-06-16
4. Tissue inhibitor of metalloproteinase 1 suppresses growth and differentiation of osteoblasts and differentiation of osteoclasts by targeting the AKT pathway;Experimental Cell Research;2020-04
5. Extracellular matrix, regional heterogeneity of the aorta, and aortic aneurysm;Experimental & Molecular Medicine;2019-12
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