The specificity of TIMP-2 for matrix metalloproteinases can be modified by single amino acid mutations (Q77985332)

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10 December 2019

title

The specificity of TIMP-2 for matrix metalloproteinases can be modified by single amino acid mutations (English)

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10 December 2019

5

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10 December 2019

author name string

G S Butler

1

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10 December 2019

M Hutton

2

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10 December 2019

B A Wattam

3

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10 December 2019

R A Williamson

4

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10 December 2019

F Willenbrock

6

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10 December 2019

G Murphy

7

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10 December 2019

language of work or name

English

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publication date

1 July 1999

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Journal of Biological Chemistry

10 December 2019

published in

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10 December 2019

volume

274

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10 December 2019

issue

29

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10 December 2019

page(s)

20391-20396

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Mechanisms of connective tissue matrix destruction in periodontitis

10 December 2019

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Cloning of the cDNA encoding human tissue inhibitor of metalloproteinases-3 (TIMP-3) and mapping of the TIMP3 gene to chromosome 22

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Molecular cloning and characterization of human tissue inhibitor of metalloproteinase 4

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Disulphide bond assignment in human tissue inhibitor of metalloproteinases (TIMP)

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Computational sequence analysis of the tissue inhibitor of metalloproteinase family

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Kinetic analysis of the mechanism of interaction of full-length TIMP-2 and gelatinase A: evidence for the existence of a low-affinity intermediate

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Mechanism of cell surface activation of 72-kDa type IV collagenase. Isolation of the activated form of the membrane metalloprotease

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The soluble catalytic domain of membrane type 1 matrix metalloproteinase cleaves the propeptide of progelatinase A and initiates autoproteolytic activation. Regulation by TIMP-2 and TIMP-3.

21 January 2018

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Folding and stability of the active N-terminal domain of tissue inhibitor of metalloproteinases-1 and -2.

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The N-terminal domain of tissue inhibitor of metalloproteinases retains metalloproteinase inhibitory activity

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Characterization of the functional domain of tissue inhibitor of metalloproteinases-2 (TIMP-2).

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The activity of the tissue inhibitors of metalloproteinases is regulated by C-terminal domain interactions: a kinetic analysis of the inhibition of gelatinase A.

21 January 2018

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Different domain interactions are involved in the binding of tissue inhibitors of metalloproteinases to stromelysin-1 and gelatinase A

21 January 2018

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Mapping the binding site for matrix metalloproteinase on the N-terminal domain of the tissue inhibitor of metalloproteinases-2 by NMR chemical shift perturbation

21 January 2018

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Mechanism of inhibition of the human matrix metalloproteinase stromelysin-1 by TIMP-1

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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

21 January 2018

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Solution structure of the active domain of tissue inhibitor of metalloproteinases-2. A new member of the OB fold protein family

21 January 2018

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High resolution structure of the N-terminal domain of tissue inhibitor of metalloproteinases-2 and characterization of its interaction site with matrix metalloproteinase-3

21 January 2018

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Mutational study of the amino-terminal domain of human tissue inhibitor of metalloproteinases 1 (TIMP-1) locates an inhibitory region for matrix metalloproteinases

21 January 2018

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Chemically and conformationally authentic active domain of human tissue inhibitor of metalloproteinases-2 refolded from bacterial inclusion bodies.

21 January 2018

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Site-directed mutagenesis by overlap extension using the polymerase chain reaction

21 January 2018

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Purification of recombinant human prostromelysin. Studies on heat activation to give high-Mr and low-Mr active forms, and a comparison of recombinant with natural stromelysin activities

21 January 2018

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Biochemical characterization of matrilysin. Activation conforms to the stepwise mechanisms proposed for other matrix metalloproteinases

21 January 2018

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The C-terminal domain of 72 kDa gelatinase A is not required for catalysis, but is essential for membrane activation and modulates interactions with tissue inhibitors of metalloproteinases

21 January 2018

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Biochemical characterization of human collagenase-3

21 January 2018

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Collagenase 2 (MMP-8) expression in murine tissue-remodeling processes. Analysis of its potential role in postpartum involution of the uterus.

21 January 2018

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Membrane-type matrix metalloproteinases 1 and 2 exhibit broad-spectrum proteolytic capacities comparable to many matrix metalloproteinases

21 January 2018

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A novel coumarin-labelled peptide for sensitive continuous assays of the matrix metalloproteinases

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Site-directed mutations that alter the inhibitory activity of the tissue inhibitor of metalloproteinases-1: importance of the N-terminal region between cysteine 3 and cysteine 13

21 January 2018

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Involvement of a region near valine-69 of tissue inhibitor of metalloproteinases (TIMP)-1 in the interaction with matrix metalloproteinase 3 (stromelysin 1).

21 January 2018

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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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21 January 2018

Identifiers

DOI

10.1074/JBC.274.29.20391

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:10400663%20AND%20SRC:MED&resulttype=core&format=json

10 December 2019

1 reference