Reactome: A Curated Pathway Database

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Pathways reviewed by Butler, GS (1592354)

DB_ID Name
1592389 Activation of Matrix Metalloproteinases

Details on Person Butler, GS

Class:IdPerson:1592354
_displayNameButler, GS
_timestamp2017-08-22 20:43:40
created[InstanceEdit:1592294] Jupe, S, 2011-09-09
initialGS
surnameButler
(author)[LiteratureReference:1592332] The TIMP2 membrane type 1 metalloproteinase "receptor" regulates the concentration and efficient activation of progelatinase A. A kinetic study
[LiteratureReference:1592360] Membrane-type-2 matrix metalloproteinase can initiate the processing of progelatinase A and is regulated by the tissue inhibitors of metalloproteinases
[LiteratureReference:2157484] Tissue inhibitor of metalloproteinases-4 inhibits but does not support the activation of gelatinase A via efficient inhibition of membrane type 1-matrix metalloproteinase
[LiteratureReference:2157493] Collagen binding properties of the membrane type-1 matrix metalloproteinase (MT1-MMP) hemopexin C domain. The ectodomain of the 44-kDa autocatalytic product of MT1-MMP inhibits cell invasion by disrupting native type I collagen cleavage
[LiteratureReference:2157495] Utilization of a novel recombinant myoglobin fusion protein expression system to characterize the tissue inhibitor of metalloproteinase (TIMP)-4 and TIMP-2 C-terminal domain and tails by mutagenesis. The importance of acidic residues in binding the MMP-2 hemopexin C-domain
[LiteratureReference:2157500] Cellular activation of MMP-2 (gelatinase A) by MT2-MMP occurs via a TIMP-2-independent pathway
[LiteratureReference:2157522] Updated biological roles for matrix metalloproteinases and new "intracellular" substrates revealed by degradomics
[LiteratureReference:2157525] Matrix metalloproteinase proteomics: substrates, targets, and therapy
[InstanceEdit:2157481] Butler, GS, 2012-02-28
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