The hemopexin-like C-terminal domain of membrane type 1 matrix metalloproteinase regulates proteolysis of a multifunctional protein, gC1qR
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Matrix metalloproteinases: old dogs with new tricksA role for the mitochondrial-associated protein p32 in regulation of trophoblast proliferation.Clusterin, an abundant serum factor, is a possible negative regulator of MT6-MMP/MMP-25 produced by neutrophils.Microarray and proteomic analysis of breast cancer cell and osteoblast co-cultures: role of osteoblast matrix metalloproteinase (MMP)-13 in bone metastasis.Matrix metalloproteinase inhibitors as investigative tools in the pathogenesis and management of vascular disease.SheddomeDB: the ectodomain shedding database for membrane-bound shed markers.Matrix metalloproteinases as potential targets in the venous dilation associated with varicose veins.Pharmacoproteomics of a metalloproteinase hydroxamate inhibitor in breast cancer cells: dynamics of membrane type 1 matrix metalloproteinase-mediated membrane protein sheddingDistinct functions for the catalytic and hemopexin domains of a Drosophila matrix metalloproteinase.Molecular signature of MT1-MMP: transactivation of the downstream universal gene network in cancer.Soluble gC1qR is an autocrine signal that induces B1R expression on endothelial cells.Matrix metalloproteinases and their role in oncogenesis: a review.Matrix metalloproteinase processing of signaling molecules to regulate inflammation.Cellular membrane type-1 matrix metalloproteinase (MT1-MMP) cleaves C3b, an essential component of the complement system.Distinct roles of catalytic and pexin-like domains in membrane-type matrix metalloproteinase (MMP)-mediated pro-MMP-2 activation and collagenolysis.Non-proteolytic, receptor/ligand interactions associate cellular membrane type-1 matrix metalloproteinase with the complement component C1q.Membrane type-1 matrix metalloproteinase functions as a proprotein self-convertase. Expression of the latent zymogen in Pichia pastoris, autolytic activation, and the peptide sequence of the cleavage forms.Multi-functional, multicompartmental hyaluronan-binding protein 1 (HABP1/p32/gC1qR): implication in cancer progression and metastasis.
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P2860
The hemopexin-like C-terminal domain of membrane type 1 matrix metalloproteinase regulates proteolysis of a multifunctional protein, gC1qR
description
2002 թուականի Մարտին հրատարակուած գիտական յօդուած
@hyw
2002 թվականի մարտին հրատարակված գիտական հոդված
@hy
article publié dans la revue scientifique Journal of Biological Chemistry
@fr
artículu científicu espublizáu en 2002
@ast
im März 2002 veröffentlichter wissenschaftlicher Artikel
@de
scientific article (publication date: 15 March 2002)
@en
vedecký článok (publikovaný 2002/03/15)
@sk
vědecký článek publikovaný v roce 2002
@cs
wetenschappelijk artikel (gepubliceerd op 2002/03/15)
@nl
наукова стаття, опублікована в березні 2002
@uk
name
The hemopexin-like C-terminal ...... multifunctional protein, gC1qR
@ast
The hemopexin-like C-terminal ...... multifunctional protein, gC1qR
@en
The hemopexin-like C-terminal ...... multifunctional protein, gC1qR
@nl
type
label
The hemopexin-like C-terminal ...... multifunctional protein, gC1qR
@ast
The hemopexin-like C-terminal ...... multifunctional protein, gC1qR
@en
The hemopexin-like C-terminal ...... multifunctional protein, gC1qR
@nl
prefLabel
The hemopexin-like C-terminal ...... multifunctional protein, gC1qR
@ast
The hemopexin-like C-terminal ...... multifunctional protein, gC1qR
@en
The hemopexin-like C-terminal ...... multifunctional protein, gC1qR
@nl
P2093
P2860
P356
P1476
The hemopexin-like C-terminal ...... multifunctional protein, gC1qR
@en
P2093
Andreas Eichinger
Berhane Ghebrehiwet
Dmitry V Rozanov
Elena I Deryugina
Tatiana I Postnova
P2860
P304
P356
10.1074/JBC.M110711200
P407
P577
2001-12-31T00:00:00Z