Structure of the catalytic domain of human fibroblast collagenase complexed with an inhibitor
about
Biochemical characterization of human collagenase-3The role of the C-terminal domain of human collagenase-3 (MMP-13) in the activation of procollagenase-3, substrate specificity, and tissue inhibitor of metalloproteinase interactionThe metzincins--topological and sequential relations between the astacins, adamalysins, serralysins, and matrixins (collagenases) define a superfamily of zinc-peptidasesX-ray structure of human stromelysin catalytic domain complexed with nonpeptide inhibitors: Implications for inhibitor selectivityProbing the Role of Divalent Metal Ions in a Bacterial Psychrophilic Metalloprotease: Binding Studies of an Enzyme in the Crystalline State by X-Ray CrystallographyStructural insights into triple-helical collagen cleavage by matrix metalloproteinase 1Structure of collagenase G reveals a chew-and-digest mechanism of bacterial collagenolysisX-ray structures of human neutrophil collagenase complexed with peptide hydroxamate and peptide thiol inhibitors. Implications for substrate binding and rational drug designStructural interaction of natural and synthetic inhibitors with the venom metalloproteinase, atrolysin C (form d)Batimastat, a potent matrix mealloproteinase inhibitor, exhibits an unexpected mode of binding.The structure of the Aeromonas proteolytica aminopeptidase complexed with a hydroxamate inhibitor. Involvement in catalysis of Glu151 and two zinc ions of the co-catalytic unit1.8-A crystal structure of the catalytic domain of human neutrophil collagenase (matrix metalloproteinase-8) complexed with a peptidomimetic hydroxamate primed-side inhibitor with a distinct selectivity profileHydrolysis of triple-helical collagen peptide models by matrix metalloproteinasesStructural differences of matrix metalloproteinases. Homology modeling and energy minimization of enzyme-substrate complexesHydrolysis of a broad spectrum of extracellular matrix proteins by human macrophage elastaseBinary image representation of a ligand binding site: its application to efficient sampling of a conformational ensembleStructure of malonic acid-based inhibitors bound to human neutrophil collagenase. A new binding mode explains apparently anomalous data.Matrix metalloproteinases and collagen catabolism.Triple-helical peptide analysis of collagenolytic protease activity.Proteolytic host cell enzymes in gingival crevice fluid.Structural basis of the matrix metalloproteinases and their physiological inhibitors, the tissue inhibitors of metalloproteinases.Cell surface collagenolysis requires homodimerization of the membrane-bound collagenase MT1-MMPMatrix metalloproteinase inhibitors as investigative tools in the pathogenesis and management of vascular disease.Solution structure of the catalytic domain of human stromelysin complexed with a hydrophobic inhibitor.Matrix metalloproteinases as potential targets in the venous dilation associated with varicose veins.Mapping intermolecular interactions and active site conformations: from human MMP-1 crystal structure to molecular dynamics free energy calculations.New biochemical insight of conserved water molecules at catalytic and structural Zn2+ ions in human matrix metalloproteinase-I: a study by MD-simulation.Collagenase: a key enzyme in collagen turnover.Stromelysin-1: three-dimensional structure of the inhibited catalytic domain and of the C-truncated proenzyme.Squaric acid-based peptidic inhibitors of matrix metalloprotease-1.Structural characterizations of nonpeptidic thiadiazole inhibitors of matrix metalloproteinases reveal the basis for stromelysin selectivity.Solution structures of stromelysin complexed to thiadiazole inhibitors.Involvement of fibronectin type II repeats in the efficient inhibition of gelatinases A and B by long-chain unsaturated fatty acids.Pyrimidine-2,4,6-Triones: a new effective and selective class of matrix metalloproteinase inhibitors.Effect of species differences on stromelysin-1 (MMP-3) inhibitor potency. An explanation of inhibitor selectivity using homology modeling and chimeric proteins.Purification and cloning of an endogenous protein inhibitor of carp nephrosin, an astacin metalloproteinase.Hydroxamate derivatives of substrate-analogous peptides containing aminomalonic acid are potent inhibitors of matrix metalloproteinases.Chemically and conformationally authentic active domain of human tissue inhibitor of metalloproteinases-2 refolded from bacterial inclusion bodies.Specific amino acid substitutions in human collagenase cause decreased autoproteolysis and reveal a requirement for a second zinc atom for catalytic activity.
P2860
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P2860
Structure of the catalytic domain of human fibroblast collagenase complexed with an inhibitor
description
1994 nî lūn-bûn
@nan
1994 թուականի Փետրուարին հրատարակուած գիտական յօդուած
@hyw
1994 թվականի փետրվարին հրատարակված գիտական հոդված
@hy
1994年の論文
@ja
1994年論文
@yue
1994年論文
@zh-hant
1994年論文
@zh-hk
1994年論文
@zh-mo
1994年論文
@zh-tw
1994年论文
@wuu
name
Structure of the catalytic dom ...... se complexed with an inhibitor
@ast
Structure of the catalytic dom ...... se complexed with an inhibitor
@en
Structure of the catalytic dom ...... se complexed with an inhibitor
@nl
type
label
Structure of the catalytic dom ...... se complexed with an inhibitor
@ast
Structure of the catalytic dom ...... se complexed with an inhibitor
@en
Structure of the catalytic dom ...... se complexed with an inhibitor
@nl
prefLabel
Structure of the catalytic dom ...... se complexed with an inhibitor
@ast
Structure of the catalytic dom ...... se complexed with an inhibitor
@en
Structure of the catalytic dom ...... se complexed with an inhibitor
@nl
P2093
P2860
P356
P1476
Structure of the catalytic dom ...... se complexed with an inhibitor
@en
P2093
D H Williams
E J Murray
F K Winkler
M J Broadhurst
N Borkakoti
W H Johnson
P2860
P304
P356
10.1038/NSB0294-106
P577
1994-02-01T00:00:00Z