Structural properties of matrix metalloproteinases

Bode W, Fernandez-Catalan C, Tschesche H, Grams F, Nagase H, Maskos K (1999)
CELLULAR AND MOLECULAR LIFE SCIENCES 55(4): 639-652.

Journal Article | Published | English

No fulltext has been uploaded

Author
; ; ; ; ;
Abstract
Matrix metalloproteinases (MMPs) are involved in extracellular matrix degradation. Their proteolytic activity must. be precisely regulated by their endogenous protein inhibitors, the tissue inhibitors of metalloproteinases (TIMPs). Disruption of this balance results in serious diseases such as arthritis, tumour growth and metastasis. Knowledge of the tertiary structures of the proteins involved is crucial for understanding their functional properties and interference with associated dysfunctions. Within the last few years, several three-dimensional MMP and MMP-TIMP structures became available, showing the domain organization, polypeptide fold and main specificity determinants. Complexes of the catalytic MMP domains with various synthetic inhibitors enabled the structure-based design and improvement of high-affinity ligands, which might be elaborated into drugs. A multitude of reviews surveying work done on all aspects of MMPs have appeared in recent years, but none of them has focused on the three-dimensional structures. This review was written to close the gap.
Publishing Year
ISSN
eISSN
PUB-ID

Cite this

Bode W, Fernandez-Catalan C, Tschesche H, Grams F, Nagase H, Maskos K. Structural properties of matrix metalloproteinases. CELLULAR AND MOLECULAR LIFE SCIENCES. 1999;55(4):639-652.
Bode, W., Fernandez-Catalan, C., Tschesche, H., Grams, F., Nagase, H., & Maskos, K. (1999). Structural properties of matrix metalloproteinases. CELLULAR AND MOLECULAR LIFE SCIENCES, 55(4), 639-652.
Bode, W., Fernandez-Catalan, C., Tschesche, H., Grams, F., Nagase, H., and Maskos, K. (1999). Structural properties of matrix metalloproteinases. CELLULAR AND MOLECULAR LIFE SCIENCES 55, 639-652.
Bode, W., et al., 1999. Structural properties of matrix metalloproteinases. CELLULAR AND MOLECULAR LIFE SCIENCES, 55(4), p 639-652.
W. Bode, et al., “Structural properties of matrix metalloproteinases”, CELLULAR AND MOLECULAR LIFE SCIENCES, vol. 55, 1999, pp. 639-652.
Bode, W., Fernandez-Catalan, C., Tschesche, H., Grams, F., Nagase, H., Maskos, K.: Structural properties of matrix metalloproteinases. CELLULAR AND MOLECULAR LIFE SCIENCES. 55, 639-652 (1999).
Bode, W, Fernandez-Catalan, C, Tschesche, Harald, Grams, F, Nagase, H, and Maskos, K. “Structural properties of matrix metalloproteinases”. CELLULAR AND MOLECULAR LIFE SCIENCES 55.4 (1999): 639-652.
This data publication is cited in the following publications:
This publication cites the following data publications:

98 Citations in Europe PMC

Data provided by Europe PubMed Central.

ADAMTS13 and von Willebrand factor interactions.
Zander CB, Cao W, Zheng XL., Curr. Opin. Hematol. 22(5), 2015
PMID: 26186678
Ascorbyl coumarates as multifunctional cosmeceutical agents that inhibit melanogenesis and enhance collagen synthesis.
Kwak JY, Park S, Seok JK, Liu KH, Boo YC., Arch. Dermatol. Res. 307(7), 2015
PMID: 26078014
Characterization of MMP-9 gene from a normalized cDNA library of kidney tissue of yellow catfish (Pelteobagrus fulvidraco).
Ke F, Wang Y, Hong J, Xu C, Chen H, Zhou SB., Fish Shellfish Immunol. 45(2), 2015
PMID: 25910849
Association of MMP-9 gene polymorphisms with Behcet's disease risk.
Naouali A, Kaabachi W, Tizaoui K, Amor AB, Hamzaoui A, Hamzaoui K., Immunol. Lett. 164(1), 2015
PMID: 25639450
Implication of matrix metalloproteinases in regulating neuronal disorder.
Mukherjee A, Swarnakar S., Mol. Biol. Rep. 42(1), 2015
PMID: 25374425
Characterization of selective exosite-binding inhibitors of matrix metalloproteinase 13 that prevent articular cartilage degradation in vitro.
Spicer TP, Jiang J, Taylor AB, Choi JY, Hart PJ, Roush WR, Fields GB, Hodder PS, Minond D., J. Med. Chem. 57(22), 2014
PMID: 25330343
Functional polymorphisms of matrix metalloproteinase-9 and survival in patients with locoregionally advanced nasopharyngeal carcinoma treated with chemoradiotherapy.
Liu H, Huang PY, Tang LQ, Chen QY, Zhang Y, Zhang L, Guo L, Luo DH, Mo HY, Xiang YQ, Qiu F, Sun R, Chen MY, Hua YJ, Lv X, Wang L, Zhao C, Guo X, Cao KJ, Qian CN, Hong MH, Mai HQ., Med. Oncol. 30(4), 2013
PMID: 23955812
Matrix metalloproteinase inhibitors based on the 3-mercaptopyrrolidine core.
Jin Y, Roycik MD, Bosco DB, Cao Q, Constantino MH, Schwartz MA, Sang QX., J. Med. Chem. 56(11), 2013
PMID: 23631440
High enrichment of MMP-9 and carboxypeptidase A by tweezing adsorptive bubble separation (TABS).
Haller D, Ekici P, Friess A, Parlar H., Appl. Biochem. Biotechnol. 162(6), 2010
PMID: 20229282
Solution structure of wild-type human matrix metalloproteinase 12 (MMP-12) in complex with a tight-binding inhibitor.
Markus MA, Dwyer B, Wolfrom S, Li J, Li W, Malakian K, Wilhelm J, Tsao DH., J. Biomol. NMR 41(1), 2008
PMID: 18425585
A peptide hydroxamate library for enrichment of metalloproteinases: towards an affinity-based metalloproteinase profiling protocol.
Geurink P, Klein T, Leeuwenburgh M, van der Marel G, Kauffman H, Bischoff R, Overkleeft H., Org. Biomol. Chem. 6(7), 2008
PMID: 18362965
MT1-MMP shedding involves an ADAM and is independent of its localization in lipid rafts.
Toth M, Sohail A, Mobashery S, Fridman R., Biochem. Biophys. Res. Commun. 350(2), 2006
PMID: 17007816
Modulation of collagen metabolism by the nucleolar protein fibrillarin.
Lefevre F, Garnotel R, Georges N, Gillery P., Exp. Cell Res. 271(1), 2001
PMID: 11697885
Expression of human membrane type 1 matrix metalloproteinase in Pichia pastoris.
Roderfeld M, Buttner FH, Bartnik E, Tschesche H., Protein Expr. Purif. 19(3), 2000
PMID: 10910727

Export

0 Marked Publications

Open Data PUB

Web of Science

View record in Web of Science®

Sources

PMID: 10357232
PubMed | Europe PMC

Search this title in

Google Scholar