Human fibroblast stromelysin catalytic domain: expression, purification, and characterization of a C-terminally truncated form.
about
X-ray structure of a novel matrix metalloproteinase inhibitor complexed to stromelysinMatrix Metalloproteinase-10 (MMP-10) Interaction with Tissue Inhibitors of Metalloproteinases TIMP-1 and TIMP-2: BINDING STUDIES AND CRYSTAL STRUCTUREHigh resolution structure of the N-terminal domain of tissue inhibitor of metalloproteinases-2 and characterization of its interaction site with matrix metalloproteinase-3Metalloproteinase Activity Secreted by Fibrogenic Cells in the Processing of Prolysyl OxidaseCritical role of glutamic acid 202 in the enzymatic activity of stromelysin-1 (MMP-3).Production of active mammalian and viral proteases in bacterial expression systems.Formation of a covalent Hg-Cys-bond during mercurial activation of PMNL procollagenase gives evidence of a cysteine-switch mechanism.Bioactive conformation of stromelysin inhibitors determined by transferred nuclear Overhauser effects.Expression of matrix metalloproteinase-9 in human platelets: regulation of platelet activation in in vitro and in vivo studiesThe matrix metalloproteinases and their inhibitors.Cloning of a 72 kDa matrix metalloproteinase (gelatinase) from chicken embryo fibroblasts using gene family PCR: expression of the gelatinase increases upon malignant transformation.Reversal of TREM-1 ectodomain shedding and improved bacterial clearance by intranasal metalloproteinase inhibitors.A single step purification for autolytic zinc proteinases.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.Stromelysin-1: three-dimensional structure of the inhibited catalytic domain and of the C-truncated proenzyme.Fragmentation of human polymorphonuclear-leucocyte collagenase.Structural characterizations of nonpeptidic thiadiazole inhibitors of matrix metalloproteinases reveal the basis for stromelysin selectivity.Effect of species differences on stromelysin-1 (MMP-3) inhibitor potency. An explanation of inhibitor selectivity using homology modeling and chimeric proteins.Cloning of rat 92-kDa type IV collagenase and expression of an active recombinant catalytic domain.Identification of structural determinants controlling human and mouse stromelysin-3 proteolytic activities.The hemopexin-like domain (C domain) of human gelatinase A (matrix metalloproteinase-2) requires Ca2+ for fibronectin and heparin binding. Binding properties of recombinant gelatinase A C domain to extracellular matrix and basement membrane componenInactivation of plasminogen activator inhibitor-1 by specific proteolysis with stromelysin-1 (MMP-3).
P2860
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P2860
Human fibroblast stromelysin catalytic domain: expression, purification, and characterization of a C-terminally truncated form.
description
1991 nî lūn-bûn
@nan
1991年の論文
@ja
1991年学术文章
@wuu
1991年学术文章
@zh-cn
1991年学术文章
@zh-hans
1991年学术文章
@zh-my
1991年学术文章
@zh-sg
1991年學術文章
@yue
1991年學術文章
@zh
1991年學術文章
@zh-hant
name
Human fibroblast stromelysin c ...... a C-terminally truncated form.
@en
type
label
Human fibroblast stromelysin c ...... a C-terminally truncated form.
@en
prefLabel
Human fibroblast stromelysin c ...... a C-terminally truncated form.
@en
P2093
P356
P1433
P1476
Human fibroblast stromelysin c ...... a C-terminally truncated form.
@en
P2093
Boulton DA
Cameron PM
Eiberger LL
Hagmann WK
Harrison R
Hutchinson NI
P304
P356
10.1021/BI00240A018
P407
P577
1991-07-01T00:00:00Z