Matrix metalloproteinases (MMPs): Chemical–biological functions and (Q) SARs
RP Verma, C Hansch - Bioorganic & medicinal chemistry, 2007 - Elsevier
Matrix metalloproteinases (MMPs) are a large family of calcium-dependent zinc-containing
endopeptidases, which are responsible for the tissue remodeling and degradation of the …
endopeptidases, which are responsible for the tissue remodeling and degradation of the …
Design and Therapeutic Application of Matrix Metalloproteinase Inhibitors. (Chem. Rev. 1999, 99, 2735−2776. Published on the Web September 8, 1999).
M Whittaker, CD Floyd, P Brown, AJH Gearing - Chemical reviews, 2001 - ACS Publications
Determination of protease cleavage site motifs using mixture-based oriented peptide libraries
BE Turk, LL Huang, ET Piro, LC Cantley - Nature biotechnology, 2001 - nature.com
The number of known proteases is increasing at a tremendous rate as a consequence of
genome sequencing projects. Although one can guess at the functions of these novel …
genome sequencing projects. Although one can guess at the functions of these novel …
Protease‐activated prodrugs: strategies, challenges, and future directions
M Poreba - The FEBS journal, 2020 - Wiley Online Library
Proteases play critical roles in virtually all biological processes, including proliferation, cell
death and survival, protein turnover, and migration. However, when dysregulated, these …
death and survival, protein turnover, and migration. However, when dysregulated, these …
[HTML][HTML] Crystal structure of the complex formed by the membrane type 1‐matrix metalloproteinase with the tissue inhibitor of metalloproteinases‐2, the soluble …
C Fernandez‐Catalan, W Bode, R Huber, D Turk… - The EMBO …, 1998 - embopress.org
The proteolytic activity of matrix metalloproteinases (MMPs) towards extracellular matrix
components is held in check by the tissue inhibitors of metalloproteinases (TIMPs). The …
components is held in check by the tissue inhibitors of metalloproteinases (TIMPs). The …
Matrix metalloproteinases in lung biology
WC Parks, SD Shapiro - Respiratory research, 2000 - Springer
Despite much information on their catalytic properties and gene regulation, we actually know
very little of what matrix metalloproteinases (MMPs) do in tissues. The catalytic activity of …
very little of what matrix metalloproteinases (MMPs) do in tissues. The catalytic activity of …
Epilysin, a novel human matrix metalloproteinase (MMP-28) expressed in testis and keratinocytes and in response to injury
J Lohi, CL Wilson, JD Roby, WC Parks - Journal of Biological Chemistry, 2001 - ASBMB
We have cloned a new human matrix metalloproteinase (MMP-28, epilysin) from human
keratinocyte and testis cDNA libraries. Like most MMPs, epilysin contains a signal …
keratinocyte and testis cDNA libraries. Like most MMPs, epilysin contains a signal …
Matrix-metalloproteinases as targets for controlled delivery in cancer: An analysis of upregulation and expression
KJ Isaacson, MM Jensen, NB Subrahmanyam… - Journal of Controlled …, 2017 - Elsevier
While commonly known for degradation of the extracellular matrix, matrix metalloproteinases
(MMPs) exhibit broad potential for use in targeting of bioactive and imaging agents in cancer …
(MMPs) exhibit broad potential for use in targeting of bioactive and imaging agents in cancer …
Membrane type-matrix metalloproteinases (MT-MMP)
S Zucker, D Pei, J Cao, C Lopez-Otin - 2003 - Elsevier
Membrane Type-Matrix Metalloproteinases (MT-MMP) Page 1 02/20/2003 10:46 AM
Developmental Biology-V. 54/7118F PS160-01.tex PS160-01.xml APserialsv2(2000/12/19) …
Developmental Biology-V. 54/7118F PS160-01.tex PS160-01.xml APserialsv2(2000/12/19) …
Expression of stromelysin-3 in atherosclerotic lesions: regulation via CD40–CD40 ligand signaling in vitro and in vivo
U Schönbeck, F Mach, GK Sukhova… - The Journal of …, 1999 - rupress.org
Stromelysin-3 is an unusual matrix metalloproteinase, being released in the active rather
than zymogen form and having a distinct substrate specificity, targeting serine proteinase …
than zymogen form and having a distinct substrate specificity, targeting serine proteinase …