Selective involvement of TIMP-2 in the second activational cleavage of pro-MMP-2: refinement of the pro-MMP-2 activation mechanism (Q40624145)

22 September 2017

Selective involvement of TIMP-2 in the second activational cleavage of pro-MMP-2: refinement of the pro-MMP-2 activation mechanism (English)

1 reference

22 September 2017

3

1 reference

22 September 2017

Marc A Lafleur

1

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PubMed ID

14572669

22 September 2017

Angus M Tester

series ordinal

2

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PubMed ID

14572669

22 September 2017

language of work or name

English

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publication date

1 October 2003

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22 September 2017

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22 September 2017

553

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22 September 2017

3

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22 September 2017

457-463

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New functions for the matrix metalloproteinases in cancer progression

22 September 2017

1 reference

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Role of the matrix metalloproteinase and plasminogen activator-plasmin systems in angiogenesis.

21 January 2018

1 reference

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Tissue inhibitors of metalloproteinases: evolution, structure and function

21 January 2018

1 reference

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Intermolecular autolytic cleavage can contribute to the activation of progelatinase A by cell membranes

21 January 2018

1 reference

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The TIMP2 membrane type 1 metalloproteinase "receptor" regulates the concentration and efficient activation of progelatinase A. A kinetic study

21 January 2018

1 reference

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TIMP-2 promotes activation of progelatinase A by membrane-type 1 matrix metalloproteinase immobilized on agarose beads

21 January 2018

1 reference

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

21 January 2018

1 reference

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Homophilic complex formation of MT1-MMP facilitates proMMP-2 activation on the cell surface and promotes tumor cell invasion.

21 January 2018

1 reference

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Oligomerization through hemopexin and cytoplasmic domains regulates the activity and turnover of membrane-type 1 matrix metalloproteinase

21 January 2018

1 reference

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Mutation analysis of membrane type-1 matrix metalloproteinase (MT1-MMP). The role of the cytoplasmic tail Cys(574), the active site Glu(240), and furin cleavage motifs in oligomerization, processing, and self-proteolysis of MT1-MMP expressed in brea

21 January 2018

1 reference

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Inactivating mutation of the mouse tissue inhibitor of metalloproteinases-2(Timp-2) gene alters proMMP-2 activation

21 January 2018

1 reference

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TIMP-2 is required for efficient activation of proMMP-2 in vivo

21 January 2018

1 reference

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Complex pattern of membrane type 1 matrix metalloproteinase shedding. Regulation by autocatalytic cells surface inactivation of active enzyme

21 January 2018

1 reference

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Cellular activation of MMP-2 (gelatinase A) by MT2-MMP occurs via a TIMP-2-independent pathway

21 January 2018

1 reference

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Domain interactions in the gelatinase A.TIMP-2.MT1-MMP activation complex. The ectodomain of the 44-kDa form of membrane type-1 matrix metalloproteinase does not modulate gelatinase A activation

21 January 2018

1 reference

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Claudin promotes activation of pro-matrix metalloproteinase-2 mediated by membrane-type matrix metalloproteinases

21 January 2018

1 reference

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Reactive site-modified tissue inhibitor of metalloproteinases-2 inhibits the cell-mediated activation of progelatinase A.

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FS0014-5793%2803%2901094-9

The hemopexin-like domain (C domain) of human gelatinase A (matrix metalloproteinase-2) requires Ca2+ for fibronectin and heparin binding. Binding properties of recombinant gelatinase A C domain to extracellular matrix and basement membrane componen

21 January 2018

1 reference

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Localization of matrix metalloproteinase MMP-2 to the surface of invasive cells by interaction with integrin alpha v beta 3.

21 January 2018

1 reference

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Suppression of angiogenesis by lentiviral delivery of PEX, a noncatalytic fragment of matrix metalloproteinase 2.

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FS0014-5793%2803%2901094-9

Cell surface binding of TIMP-2 and pro-MMP-2/TIMP-2 complex

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FS0014-5793%2803%2901094-9

Mechanisms for pro matrix metalloproteinase activation.

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FS0014-5793%2803%2901094-9

Cell surface binding and activation of gelatinase A induced by expression of membrane-type-1-matrix metalloproteinase (MT1-MMP)

7 January 2021

1 reference

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Biophysical and functional characterization of full-length, recombinant human tissue inhibitor of metalloproteinases-2 (TIMP-2) produced in Escherichia coli. Comparison of wild type and amino-terminal alanine appended variant with implications for t

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0014-5793%2803%2901094-9

MT1-MMP on the cell surface causes focal degradation of gelatin films

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0014-5793%2803%2901094-9

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

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0014-5793%2803%2901094-9

Cell surface-mediated activation of progelatinase A: demonstration of the involvement of the C-terminal domain of progelatinase A in cell surface binding and activation of progelatinase A by primary fibroblasts

7 January 2021

1 reference

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Characterization of the role of the "MT-loop": an eight-amino acid insertion specific to progelatinase A (MMP2) activating membrane-type matrix metalloproteinases

7 January 2021

1 reference

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Human progelatinase A can be activated by autolysis at a rate that is concentration-dependent and enhanced by heparin bound to the C-terminal domain

7 January 2021

1 reference

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Functional activation of integrin alpha V beta 3 in tumor cells expressing membrane-type 1 matrix metalloproteinase

7 January 2021

1 reference

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10.1016/S0014-5793(03)01094-9

7 January 2021

Identifiers

DOI

1 reference

22 September 2017

1 reference

PubMed ID

14572669