Sequence motifs of tissue inhibitor of metalloproteinases 2 (TIMP-2) determining progelatinase A (proMMP-2) binding and activation by membrane-type metalloproteinase 1 (MT1-MMP).
about
Targeting matrix metalloproteinases in heart disease: lessons from endogenous inhibitorsLess is more: low expression of MT1-MMP is optimal to promote migration and tumourigenesis of breast cancer cells.Plasma levels of MMP-7 and TIMP-1 in laboratory diagnostics and differentiation of selected histological types of epithelial ovarian cancers.Direct expression of active human tissue inhibitors of metalloproteinases by periplasmic secretion in Escherichia coli.The tissue inhibitors of metalloproteinases (TIMPs): an ancient family with structural and functional diversityIdentification of fetal and maternal single nucleotide polymorphisms in candidate genes that predispose to spontaneous preterm labor with intact membranes.ADAMTS4 (aggrecanase-1) activation on the cell surface involves C-terminal cleavage by glycosylphosphatidyl inositol-anchored membrane type 4-matrix metalloproteinase and binding of the activated proteinase to chondroitin sulfate and heparan sulfateThe α7-nicotinic acetylcholine receptor and MMP-2/-9 pathway mediate the proangiogenic effect of nicotine in human retinal endothelial cells.Endothelial cell microparticles act as centers of matrix metalloproteinsase-2 (MMP-2) activation and vascular matrix remodeling.Filamin A controls matrix metalloproteinase activity and regulates cell invasion in human fibrosarcoma cells.Control of matrix metalloproteinase catalytic activityOxidative stress and the development of diabetic retinopathy: contributory role of matrix metalloproteinase-2.A peptide derived from TIMP-3 inhibits multiple angiogenic growth factor receptors and tumour growth and inflammatory arthritis in mice.Matrix metalloproteinases are involved in cardiovascular diseases.Peptide from the C-terminal domain of tissue inhibitor of matrix metalloproteinases-2 (TIMP-2) inhibits membrane activation of matrix metalloproteinase-2 (MMP-2).Timp-2 binding with cellular MT1-MMP stimulates invasion-promoting MEK/ERK signaling in cancer cells.Dimerization of endogenous MT1-MMP is a regulatory step in the activation of the 72-kDa gelatinase MMP-2 on fibroblasts and fibrosarcoma cells.Individual Timp deficiencies differentially impact pro-MMP-2 activation.Mutational and structural analyses of the hinge region of membrane type 1-matrix metalloproteinase and enzyme processing.Genome-wide analysis revealed that DZNep reduces tubulointerstitial fibrosis via down-regulation of pro-fibrotic genes.
P2860
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P2860
Sequence motifs of tissue inhibitor of metalloproteinases 2 (TIMP-2) determining progelatinase A (proMMP-2) binding and activation by membrane-type metalloproteinase 1 (MT1-MMP).
description
2003 nî lūn-bûn
@nan
2003年の論文
@ja
2003年論文
@yue
2003年論文
@zh-hant
2003年論文
@zh-hk
2003年論文
@zh-mo
2003年論文
@zh-tw
2003年论文
@wuu
2003年论文
@zh
2003年论文
@zh-cn
name
Sequence motifs of tissue inhi ...... metalloproteinase 1 (MT1-MMP).
@en
Sequence motifs of tissue inhibitor of metalloproteinases 2
@nl
type
label
Sequence motifs of tissue inhi ...... metalloproteinase 1 (MT1-MMP).
@en
Sequence motifs of tissue inhibitor of metalloproteinases 2
@nl
prefLabel
Sequence motifs of tissue inhi ...... metalloproteinase 1 (MT1-MMP).
@en
Sequence motifs of tissue inhibitor of metalloproteinases 2
@nl
P2093
P2860
P50
P356
P1433
P1476
Sequence motifs of tissue inhi ...... metalloproteinase 1 (MT1-MMP)
@en
P2093
Gillian Murphy
Joanna R Worley
Meng H Lee
Mike Hutton
Philip B Thompkins
P2860
P304
P356
10.1042/BJ20021573
P407
P577
2003-06-01T00:00:00Z