MT1-MMP hemopexin domain exchange with MT4-MMP blocks enzyme maturation and trafficking to the plasma membrane in MCF7 cells (Q24685496)

From Wikidata

Jump to navigation Jump to search

scientific article

edit

Language	Label	Description	Also known as
English	MT1-MMP hemopexin domain exchange with MT4-MMP blocks enzyme maturation and trafficking to the plasma membrane in MCF7 cells	scientific article

Statements

instance of

scholarly article

0 references

title

MT1-MMP hemopexin domain exchange with MT4-MMP blocks enzyme maturation and trafficking to the plasma membrane in MCF7 cells (English)

0 references

main subject

cell biology

0 references

author name string

Susan J Atkinson

series ordinal

1

0 references

Christian Roghi

series ordinal

2

0 references

Gillian Murphy

series ordinal

3

0 references

language of work or name

English

0 references

publication date

15 August 2006

0 references

number of pages

8

1 reference

based on heuristic

inferred from page(s)

published in

Biochemical Journal

0 references

volume

398

0 references

issue

1

0 references

page(s)

15-22

0 references

cites work

Giantin, a novel conserved Golgi membrane protein containing a cytoplasmic domain of at least 350 kDa

1 reference

stated in

PubMed Central

reference URL

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1525013

retrieved

7 April 2017

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

1 reference

stated in

PubMed Central

reference URL

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1525013

retrieved

7 April 2017

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

1 reference

stated in

PubMed Central

reference URL

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1525013

retrieved

7 April 2017

The TIMP2 Membrane Type 1 Metalloproteinase “Receptor” Regulates the Concentration and Efficient Activation of Progelatinase A

1 reference

stated in

PubMed Central

reference URL

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1525013

retrieved

7 April 2017

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

1 reference

stated in

PubMed Central

reference URL

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1525013

retrieved

7 April 2017

Plasma membrane-dependent activation of the 72-kDa type IV collagenase is prevented by complex formation with TIMP-2

1 reference

stated in

PubMed Central

reference URL

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1525013

retrieved

7 April 2017

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

1 reference

stated in

PubMed Central

reference URL

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1525013

retrieved

7 April 2017

New functions for the matrix metalloproteinases in cancer progression

1 reference

stated in

PubMed Central

reference URL

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1525013

retrieved

7 April 2017

The transmembrane domain is essential for the microtubular trafficking of membrane type-1 matrix metalloproteinase (MT1-MMP).

1 reference

stated in

PubMed Central

reference URL

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1525013

retrieved

28 September 2017

The hemopexin domain of membrane-type matrix metalloproteinase-1 (MT1-MMP) Is not required for its activation of proMMP2 on cell surface but is essential for MT1-MMP-mediated invasion in three-dimensional type I collagen

1 reference

stated in

PubMed Central

reference URL

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1525013

retrieved

28 September 2017

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

1 reference

stated in

PubMed Central

reference URL

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1525013

retrieved

28 September 2017

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

1 reference

stated in

PubMed Central

reference URL

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1525013

retrieved

28 September 2017

Membrane type 4 matrix metalloproteinase (MMP17) has tumor necrosis factor-alpha convertase activity but does not activate pro-MMP2.

1 reference

stated in

PubMed Central

reference URL

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1525013

retrieved

28 September 2017

Dynamic association of cytoplasmic dynein heavy chain 1a with the Golgi apparatus and intermediate compartment.

1 reference

stated in

PubMed Central

reference URL

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1525013

retrieved

28 September 2017

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

stated in

PubMed Central

reference URL

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1525013

retrieved

28 September 2017

The 21-kDa protein is a transformation-sensitive metalloproteinase inhibitor of chicken fibroblasts

1 reference

stated in

PubMed Central

reference URL

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1525013

retrieved

30 May 2018

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

1 reference

stated in

PubMed Central

reference URL

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1525013

retrieved

30 May 2018

Membrane type I-matrix metalloproteinase (MT1-MMP) is internalised by two different pathways and is recycled to the cell surface

1 reference

stated in

PubMed Central

reference URL

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1525013

retrieved

28 November 2018

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

1 reference

stated in

PubMed Central

reference URL

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1525013

retrieved

28 November 2018

Electrophoretic analysis of plasminogen activators in polyacrylamide gels containing sodium dodecyl sulfate and copolymerized substrates

1 reference

stated in

PubMed

reference URL

https://pubmed.ncbi.nlm.nih.gov/16686598

retrieved

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

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

1 reference

stated in

PubMed

reference URL

https://pubmed.ncbi.nlm.nih.gov/16686598

retrieved

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

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

stated in

PubMed

reference URL

https://pubmed.ncbi.nlm.nih.gov/16686598

retrieved

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Presence of high levels of MT1-MMP protein in fibroblastic cells of human invasive carcinomas

1 reference

stated in

PubMed

reference URL

https://pubmed.ncbi.nlm.nih.gov/16686598

retrieved

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Murine TIMP-2 gene-targeted mutation

1 reference

stated in

PubMed

reference URL

https://pubmed.ncbi.nlm.nih.gov/16686598

retrieved

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Identifiers

DOI

10.1042/BJ20060243

0 references

PMC publication ID

1525013

0 references

PubMed publication ID

16686598

0 references

 

Sitelinks

Wikipedia(0 entries)

edit

Wikibooks(0 entries)

edit

Wikinews(0 entries)

edit

Wikiquote(0 entries)

edit

Wikisource(0 entries)

edit

Wikiversity(0 entries)

edit

Wikivoyage(0 entries)

edit

Wiktionary(0 entries)

edit

Multilingual sites(0 entries)

edit

Retrieved from "https://www.wikidata.org/w/index.php?title=Q24685496&oldid=1901772043"