Insights into MMP-TIMP interactions

Bode W, Fernandez-Catalan C, Grams F, Gomis-Ruth FX, Nagase H, Tschesche H, Maskos K (1999)
In: INHIBITION OF MATRIX METALLOPROTEINASES: THERAPEUTIC APPLICATIONS. Annals of the New York Academy of Sciences, 878. NEW YORK ACAD SCIENCES: 73-91.

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Konferenzbeitrag | Veröffentlicht | Englisch
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Abstract / Bemerkung
The proteolytic activity of the matrix metalloproteinases (MMPs) involved in extracellular matrix degradation must be precisely regulated by their endogenous protein inhibitors, the tissue inhibitors of metalloproteinases (TIMPs). Disruption of this balance can result in serious diseases such as arthritis and tumor growth and metastasis, Knowledge of the tertiary structures of the proteins involved in such processes is crucial for understanding their functional properties and to interfere with associated dysfunctions, Within the last few years, several three-dimensional structures have been determined showing the domain organization, the polypeptide fold, and the main specificity determinants of the MMPs. 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, Very recently, structural information also became available for some TIMP structures and MMP-TIMP complexes, and these new data elucidated important structural features that govern the enzyme-inhibitor interaction.
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Titel des Konferenzbandes
INHIBITION OF MATRIX METALLOPROTEINASES: THERAPEUTIC APPLICATIONS
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878
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73-91
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Bode W, Fernandez-Catalan C, Grams F, et al. Insights into MMP-TIMP interactions. In: INHIBITION OF MATRIX METALLOPROTEINASES: THERAPEUTIC APPLICATIONS. Annals of the New York Academy of Sciences. Vol 878. NEW YORK ACAD SCIENCES; 1999: 73-91.
Bode, W., Fernandez-Catalan, C., Grams, F., Gomis-Ruth, F. X., Nagase, H., Tschesche, H., & Maskos, K. (1999). Insights into MMP-TIMP interactions. INHIBITION OF MATRIX METALLOPROTEINASES: THERAPEUTIC APPLICATIONS, Annals of the New York Academy of Sciences, 878, 73-91. NEW YORK ACAD SCIENCES. doi:10.1111/j.1749-6632.1999.tb07675.x
Bode, W., Fernandez-Catalan, C., Grams, F., Gomis-Ruth, F. X., Nagase, H., Tschesche, H., and Maskos, K. (1999). “Insights into MMP-TIMP interactions” in INHIBITION OF MATRIX METALLOPROTEINASES: THERAPEUTIC APPLICATIONS Annals of the New York Academy of Sciences, vol. 878, (NEW YORK ACAD SCIENCES), 73-91.
Bode, W., et al., 1999. Insights into MMP-TIMP interactions. In INHIBITION OF MATRIX METALLOPROTEINASES: THERAPEUTIC APPLICATIONS. Annals of the New York Academy of Sciences. no.878 NEW YORK ACAD SCIENCES, pp. 73-91.
W. Bode, et al., “Insights into MMP-TIMP interactions”, INHIBITION OF MATRIX METALLOPROTEINASES: THERAPEUTIC APPLICATIONS, Annals of the New York Academy of Sciences, vol. 878, NEW YORK ACAD SCIENCES, 1999, pp.73-91.
Bode, W., Fernandez-Catalan, C., Grams, F., Gomis-Ruth, F.X., Nagase, H., Tschesche, H., Maskos, K.: Insights into MMP-TIMP interactions. INHIBITION OF MATRIX METALLOPROTEINASES: THERAPEUTIC APPLICATIONS. Annals of the New York Academy of Sciences. 878, p. 73-91. NEW YORK ACAD SCIENCES (1999).
Bode, W, Fernandez-Catalan, C, Grams, F, Gomis-Ruth, FX, Nagase, H, Tschesche, Harald, and Maskos, K. “Insights into MMP-TIMP interactions”. INHIBITION OF MATRIX METALLOPROTEINASES: THERAPEUTIC APPLICATIONS. NEW YORK ACAD SCIENCES, 1999.Vol. 878. Annals of the New York Academy of Sciences. 73-91.

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Mutational analysis of residues in and around the active site of human fibroblast-type collagenase.
Windsor LJ, Bodden MK, Birkedal-Hansen B, Engler JA, Birkedal-Hansen H., J. Biol. Chem. 269(42), 1994
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Structure of astacin and implications for activation of astacins and zinc-ligation of collagenases.
Bode W, Gomis-Ruth FX, Huber R, Zwilling R, Stocker W., Nature 358(6382), 1992
PMID: 1319561
Structure of astacin with a transition-state analogue inhibitor.
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PMID: 8756323
Crystal structure of a complex between Serratia marcescens metallo-protease and an inhibitor from Erwinia chrysanthemi.
Baumann U, Bauer M, Letoffe S, Delepelaire P, Wandersman C., J. Mol. Biol. 248(3), 1995
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The TIMP2 membrane type 1 metalloproteinase "receptor" regulates the concentration and efficient activation of progelatinase A. A kinetic study.
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