Mapping the serpin-proteinase complex using single cysteine variants of alpha1-proteinase inhibitor Pittsburgh.
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Active site distortion is sufficient for proteinase inhibition by serpins: structure of the covalent complex of alpha1-proteinase inhibitor with porcine pancreatic elastaseInactive conformation of the serpin alpha(1)-antichymotrypsin indicates two-stage insertion of the reactive loop: implications for inhibitory function and conformational diseaseCytokine response modifier a inhibition of initiator caspases results in covalent complex formation and dissociation of the caspase tetramerStructure of a serpin-enzyme complex probed by cysteine substitutions and fluorescence spectroscopy.A serpin-induced extensive proteolytic susceptibility of urokinase-type plasminogen activator implicates distortion of the proteinase substrate-binding pocket and oxyanion hole in the serpin inhibitory mechanism.Polymerization of plasminogen activator inhibitor-1.Protein misfolding and the serpinopathies.Alpha1-antitrypsin deficiency. 4: Molecular pathophysiologyFormation of the covalent serpin-proteinase complex involves translocation of the proteinase by more than 70 A and full insertion of the reactive center loop into beta-sheet A.alpha(1)-Proteinase inhibitor mutants with specificity for plasma kallikrein and C1s but not C1So how do you know you have a macromolecular complex?Kinetic intermediates en route to the final serpin-protease complex: studies of complexes of α1-protease inhibitor with trypsinEngineering functional antithrombin exosites in alpha1-proteinase inhibitor that specifically promote the inhibition of factor Xa and factor IXa.A regulatory hydrophobic area in the flexible joint region of plasminogen activator inhibitor-1, defined with fluorescent activity-neutralizing ligands. Ligand-induced serpin polymerization.Characterization of mutant neutrophil elastase in severe congenital neutropenia.Intrinsic fluorescence changes and rapid kinetics of proteinase deformation during serpin inhibition.The pH dependence of serpin-proteinase complex dissociation reveals a mechanism of complex stabilization involving inactive and active conformational states of the proteinase which are perturbable by calcium.Localization of epitopes for monoclonal antibodies to urokinase-type plasminogen activator: relationship between epitope localization and effects of antibodies on molecular interactions of the enzyme.alpha1-Proteinase inhibitor forms initial non-covalent and final covalent complexes with elastase analogously to other serpin-proteinase pairs, suggesting a common mechanism of inhibition.Lipid oxidation inactivates the anticoagulant function of protein Z-dependent protease inhibitor (ZPI).Serine and cysteine proteases are translocated to similar extents upon formation of covalent complexes with serpins. Fluorescence perturbation and fluorescence resonance energy transfer mapping of the protease binding site in CrmA complexes with graConformational studies of plasminogen activator inhibitor type 1 by fluorescence spectroscopy. Analysis of the reactive centre of inhibitory and substrate forms, and of their respective reactive-centre cleaved forms.Pathogenic α1-Antitrypsin Polymers Are Formed by Reactive Loop-β-Sheet A Linkage
P2860
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P2860
Mapping the serpin-proteinase complex using single cysteine variants of alpha1-proteinase inhibitor Pittsburgh.
description
1998 nî lūn-bûn
@nan
1998年の論文
@ja
1998年学术文章
@wuu
1998年学术文章
@zh
1998年学术文章
@zh-cn
1998年学术文章
@zh-hans
1998年学术文章
@zh-my
1998年学术文章
@zh-sg
1998年學術文章
@yue
1998年學術文章
@zh-hant
name
Mapping the serpin-proteinase ...... oteinase inhibitor Pittsburgh.
@en
Mapping the serpin-proteinase ...... oteinase inhibitor Pittsburgh.
@nl
type
label
Mapping the serpin-proteinase ...... oteinase inhibitor Pittsburgh.
@en
Mapping the serpin-proteinase ...... oteinase inhibitor Pittsburgh.
@nl
prefLabel
Mapping the serpin-proteinase ...... oteinase inhibitor Pittsburgh.
@en
Mapping the serpin-proteinase ...... oteinase inhibitor Pittsburgh.
@nl
P2860
P356
P1476
Mapping the serpin-proteinase ...... oteinase inhibitor Pittsburgh.
@en
P2093
Gettins PG
P2860
P304
15582-15589
P356
10.1074/JBC.273.25.15582
P407
P577
1998-06-01T00:00:00Z