(Q34107252)

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Internal cleavages of the autoinhibitory prodomain are required for membrane type 1 matrix metalloproteinase activation, although furin cleavage alone generates inactive proteinase.

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7 February 2020

Internal cleavages of the autoinhibitory prodomain are required for membrane type 1 matrix metalloproteinase activation, although furin cleavage alone generates inactive proteinase (English)

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Europe PubMed Central

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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:20605791%20AND%20SRC:MED&resulttype=core&format=json

7 February 2020

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7 February 2020

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Vladislav S Golubkov

1

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7 February 2020

Piotr Cieplak

2

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7 February 2020

Alexei V Chekanov

3

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7 February 2020

Boris I Ratnikov

4

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7 February 2020

Alexander E Aleshin

5

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7 February 2020

Natalya V Golubkova

6

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7 February 2020

Tatiana I Postnova

7

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7 February 2020

Ilian A Radichev

8

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7 February 2020

Dmitri V Rozanov

9

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7 February 2020

Wenhong Zhu

10

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7 February 2020

Khatereh Motamedchaboki

11

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7 February 2020

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6 July 2010

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7 February 2020

Journal of Biological Chemistry

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7 February 2020

285

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7 February 2020

36

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7 February 2020

27726-27736

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7 February 2020

Matrix metalloproteinases: regulators of the tumor microenvironment

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Plasticity of cell migration: a multiscale tuning model

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Matrix metalloproteinase proteolysis of the myelin basic protein isoforms is a source of immunogenic peptides in autoimmune multiple sclerosis

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Epigenetic control of the invasion-promoting MT1-MMP/MMP-2/TIMP-2 axis in cancer cells

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Proteolytic interstitial cell migration: a five-step process.

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5 July 2018

Progress in matrix metalloproteinase research

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The activation and physiological functions of the proprotein convertases

1 reference

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5 July 2018

Proteolysis of the membrane type-1 matrix metalloproteinase prodomain: implications for a two-step proteolytic processing and activation.

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2934640

5 July 2018

Furin regulates the intracellular activation and the uptake rate of cell surface-associated MT1-MMP.

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2934640

5 July 2018

Structure and function of matrix metalloproteinases and TIMPs

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5 July 2018

Membrane type-1 matrix metalloproteinase (MT1-MMP) exhibits an important intracellular cleavage function and causes chromosome instability

1 reference

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Crystal structures of MMPs in complex with physiological and pharmacological inhibitors

1 reference

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Matrix metalloproteinase-26 is associated with estrogen-dependent malignancies and targets alpha1-antitrypsin serpin

1 reference

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5 July 2018

Prointegrin maturation follows rapid trafficking and processing of MT1-MMP in Furin-Negative Colon Carcinoma LoVo Cells

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2934640

5 July 2018

Tools for comparative protein structure modeling and analysis

1 reference

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5 July 2018

Furin at the cutting edge: from protein traffic to embryogenesis and disease

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2934640

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Structure of the C-terminally truncated human ProMMP9, a gelatin-binding matrix metalloproteinase

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2934640

5 July 2018

The EBI SRS server--recent developments

1 reference

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5 July 2018

Membrane-type 1 matrix metalloproteinase cleaves CD44 and promotes cell migration

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2934640

5 July 2018

Regulation of membrane type-1 matrix metalloproteinase activation by proprotein convertases

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2934640

5 July 2018

Matrix metalloproteinases

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2934640

5 July 2018

Structure of human pro-matrix metalloproteinase-2: activation mechanism revealed

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2934640

5 July 2018

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

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2934640

5 July 2018

The recombinant catalytic domain of membrane-type matrix metalloproteinase-1 (MT1-MMP) induces activation of progelatinase A and progelatinase A complexed with TIMP-2.

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2934640

5 July 2018

Activation of a recombinant membrane type 1-matrix metalloproteinase (MT1-MMP) by furin and its interaction with tissue inhibitor of metalloproteinases (TIMP)-2

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2934640

5 July 2018

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.

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2934640

5 July 2018

Stromelysin-1: three-dimensional structure of the inhibited catalytic domain and of the C-truncated proenzyme

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2934640

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A matrix metalloproteinase expressed on the surface of invasive tumour cells

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

1 reference

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Furin-dependent intracellular activation of the human stromelysin-3 zymogen

1 reference

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The cysteine switch: a principle of regulation of metalloproteinase activity with potential applicability to the entire matrix metalloproteinase gene family

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Kinetics and physiologic relevance of the inactivation of alpha 1-proteinase inhibitor, alpha 1-antichymotrypsin, and antithrombin III by matrix metalloproteinases-1 (tissue collagenase), -2 (72-kDa gelatinase/type IV collagenase), and -3 (stromelys

1 reference

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1 reference

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1 reference

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Peptides based on the conserved predomain sequence of matrix metalloproteinases inhibit human stromelysin and collagenase

1 reference

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based on heuristic

inferred from PubMed ID database lookup

Potent peptide inhibitors of stromelysin based on the prodomain region of matrix metalloproteinases

1 reference

https://pubmed.ncbi.nlm.nih.gov/20605791

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Identifiers

10.1074/JBC.M110.135442

1 reference

Europe PubMed Central

PMC publication ID

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:20605791%20AND%20SRC:MED&resulttype=core&format=json

7 February 2020

PMC publication ID

1 reference

Europe PubMed Central

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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:20605791%20AND%20SRC:MED&resulttype=core&format=json

7 February 2020

PubMed publication ID

1 reference

Europe PubMed Central

PMC publication ID

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:20605791%20AND%20SRC:MED&resulttype=core&format=json

7 February 2020

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