Homophilic complex formation of MT1-MMP facilitates proMMP-2 activation on the cell surface and promotes tumor cell invasion. (Q28215016)

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:11532942%20AND%20SRC:MED&resulttype=core&format=json

10 November 2019

title

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

1 reference

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10 November 2019

main subject

invasion facilitation

1 reference

1

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10 November 2019

author name string

Takamura A

2

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10 November 2019

Ito N

3

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10 November 2019

Maru Y

4

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10 November 2019

Sato H

5

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10 November 2019

Suenaga N

6

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10 November 2019

Aoki T

7

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10 November 2019

Seiki M

8

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10 November 2019

language of work or name

English

0 references

publication date

1 September 2001

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10 November 2019

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10 November 2019

volume

20

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10 November 2019

issue

17

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10 November 2019

page(s)

4782-4793

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Epilysin, a novel human matrix metalloproteinase (MMP-28) expressed in testis and keratinocytes and in response to injury

10 November 2019

cites work

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20 March 2017

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SV40-transformed human lung fibroblasts secrete a 92-kDa type IV collagenase which is identical to that secreted by normal human macrophages

20 March 2017

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20 March 2017

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20 March 2017

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20 March 2017

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20 March 2017

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20 March 2017

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29 September 2017

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Membrane type 1 matrix metalloproteinase (MT1-MMP) cleaves the recombinant aggrecan substrate rAgg1mut at the 'aggrecanase' and the MMP sites. Characterization of MT1-MMP catabolic activities on the interglobular domain of aggrecan

29 September 2017

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Expression of matrix metalloproteinases during rat skin wound healing: evidence that membrane type-1 matrix metalloproteinase is a stromal activator of pro-gelatinase A

29 September 2017

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29 September 2017

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29 September 2017

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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.

29 September 2017

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29 September 2017

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29 September 2017

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29 September 2017

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Human 72-kilodalton type IV collagenase forms a complex with a tissue inhibitor of metalloproteases designated TIMP-2

29 September 2017

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29 September 2017

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Purification and characterization of matrix metalloproteinase 9 from U937 monocytic leukaemia and HT1080 fibrosarcoma cells

2 June 2018

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The role of the C-terminal domain in collagenase and stromelysin specificity

2 June 2018

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Flt-1, a receptor for vascular endothelial growth factor, has transforming and morphogenic potentials

2 June 2018

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Rac1 mediates type I collagen-dependent MMP-2 activation. role in cell invasion across collagen barrier

27 November 2018

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12 December 2020

Expression of membrane-type matrix metalloproteinase in human gastric carcinomas

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12 December 2020

Steps involved in activation of the pro-matrix metalloproteinase 9 (progelatinase B)-tissue inhibitor of metalloproteinases-1 complex by 4-aminophenylmercuric acetate and proteinases

1 reference

12 December 2020

Activation of the precursor of gelatinase A/72 kDa type IV collagenase/MMP-2 in lung carcinomas correlates with the expression of membrane-type matrix metalloproteinase (MT-MMP) and with lymph node metastasis

1 reference

12 December 2020

Folding and characterization of the amino-terminal domain of human tissue inhibitor of metalloproteinases-1 (TIMP-1) expressed at high yield in E. coli

1 reference

12 December 2020

The activation of ProMMP-2 (gelatinase A) by HT1080 fibrosarcoma cells is promoted by culture on a fibronectin substrate and is concomitant with an increase in processing of MT1-MMP (MMP-14) to a 45 kDa form

1 reference

12 December 2020

Plasma membrane-bound tissue inhibitor of metalloproteinases (TIMP)-2 specifically inhibits matrix metalloproteinase 2 (gelatinase A) activated on the cell surface

1 reference

12 December 2020

MT1-MMP-deficient mice develop dwarfism, osteopenia, arthritis, and connective tissue disease due to inadequate collagen turnover

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12 December 2020

Identifiers

DOI

10.1093/EMBOJ/20.17.4782

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:11532942%20AND%20SRC:MED&resulttype=core&format=json

OpenCitations bibliographic resource ID

10 November 2019

2547627

1 reference

Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:11532942%20AND%20SRC:MED&resulttype=core&format=json

10 November 2019

PubMed publication ID

11532942

1 reference