Stromelysin-1: three-dimensional structure of the inhibited catalytic domain and of the C-truncated proenzyme.
about
Biochemical characterization of the catalytic domain of human matrix metalloproteinase 19. Evidence for a role as a potent basement membrane degrading enzymeCrystal structure of full-length human collagenase 3 (MMP-13) with peptides in the active site defines exosites in the catalytic domainThe 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 interactionStructural insight into the complex formation of latent matrix metalloproteinase 2 with tissue inhibitor of metalloproteinase 2.Characterization of matrix metalloproteinase-26, a novel metalloproteinase widely expressed in cancer cells of epithelial originStructure of human procathepsin L reveals the molecular basis of inhibition by the prosegmentThe structure of the human betaII-tryptase tetramer: fo(u)r better or worseMolecular mechanisms for the conversion of zymogens to active proteolytic enzymesX-ray structure of human stromelysin catalytic domain complexed with nonpeptide inhibitors: Implications for inhibitor selectivityThe 1.8-A crystal structure of a matrix metalloproteinase 8-barbiturate inhibitor complex reveals a previously unobserved mechanism for collagenase substrate recognitionProenzyme Structure and Activation of Astacin MetallopeptidaseStructural insights into triple-helical collagen cleavage by matrix metalloproteinase 1An unexpected binding mode for a Pol II CTD peptide phosphorylated at Ser7 in the active site of the CTD phosphatase Ssu72Batimastat, a potent matrix mealloproteinase inhibitor, exhibits an unexpected mode of binding.2 angstrom X-ray structure of adamalysin II complexed with a peptide phosphonate inhibitor adopting a retro-binding modeIdentification of the (183)RWTNNFREY(191) region as a critical segment of matrix metalloproteinase 1 for the expression of collagenolytic activityStructural differences of matrix metalloproteinases. Homology modeling and energy minimization of enzyme-substrate complexesHydrolysis of a broad spectrum of extracellular matrix proteins by human macrophage elastaseExpression, structure, and function of enamel proteinasesCatalytic activities and substrate specificity of the human membrane type 4 matrix metalloproteinase catalytic domainCloning of MMP-26A multidisciplinary approach to probing enthalpy-entropy compensation and the interfacial mobility model.Critical role of glutamic acid 202 in the enzymatic activity of stromelysin-1 (MMP-3).Structure of malonic acid-based inhibitors bound to human neutrophil collagenase. A new binding mode explains apparently anomalous data.Inhibition of MMP-2 gelatinolysis by targeting exodomain-substrate interactions.Progress in matrix metalloproteinase research.Structural aspects of activation pathways of aspartic protease zymogens and viral 3C protease precursorsProteinases in developing dental enamel.Internal cleavages of the autoinhibitory prodomain are required for membrane type 1 matrix metalloproteinase activation, although furin cleavage alone generates inactive proteinase.Localizing matrix metalloproteinase activities in the pericellular environment.Structural basis of the matrix metalloproteinases and their physiological inhibitors, the tissue inhibitors of metalloproteinases.Electrostatically Embedded Many-Body Expansion for Neutral and Charged Metalloenzyme Model SystemsNitric oxide regulates matrix metalloproteinase-9 activity by guanylyl-cyclase-dependent and -independent pathwaysStatistical analysis, optimization, and prioritization of virtual screening parameters for zinc enzymes including the anthrax toxin lethal factor.The proteasome: a macromolecular assembly designed to confine proteolysis to a nanocompartment.The anti-inflammatory effects of exercise training promote atherosclerotic plaque stabilization in apolipoprotein E knockout mice with diabetic atherosclerosis.Analysis of the Errors in the Electrostatically Embedded Many-Body Expansion of the Energy and the Correlation Energy for Zn and Cd Coordination Complexes with Five and Six Ligands and Use of the Analysis to Develop a Generally Successful FragmentatNuclear magnetic resonance mapping and functional confirmation of the collagen binding sites of matrix metalloproteinase-2.ADAM-15 disintegrin-like domain structure and function.The role of Adams in Notch signaling.
P2860
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P2860
Stromelysin-1: three-dimensional structure of the inhibited catalytic domain and of the C-truncated proenzyme.
description
1995 nî lūn-bûn
@nan
1995年の論文
@ja
1995年論文
@yue
1995年論文
@zh-hant
1995年論文
@zh-hk
1995年論文
@zh-mo
1995年論文
@zh-tw
1995年论文
@wuu
1995年论文
@zh
1995年论文
@zh-cn
name
Stromelysin-1: three-dimension ...... of the C-truncated proenzyme.
@en
Stromelysin-1: three-dimension ...... of the C-truncated proenzyme.
@nl
type
label
Stromelysin-1: three-dimension ...... of the C-truncated proenzyme.
@en
Stromelysin-1: three-dimension ...... of the C-truncated proenzyme.
@nl
prefLabel
Stromelysin-1: three-dimension ...... of the C-truncated proenzyme.
@en
Stromelysin-1: three-dimension ...... of the C-truncated proenzyme.
@nl
P2093
P2860
P356
P1433
P1476
Stromelysin-1: three-dimension ...... of the C-truncated proenzyme.
@en
P2093
Burbaum JJ
Cameron PM
Fitzgerald PM
Hagmann WK
P2860
P304
P356
10.1002/PRO.5560041002
P577
1995-10-01T00:00:00Z