Importance of the release of strand 1C to the polymerization mechanism of inhibitory serpins
about
Binding of retinoic acid by the inhibitory serpin protein C inhibitorCrystallographic and Cellular Characterisation of Two Mechanisms Stabilising the Native Fold of α1-Antitrypsin: Implications for Disease and Drug DesignThe role of strand 1 of the C beta-sheet in the structure and function of alpha(1)-antitrypsinA redox-sensitive loop regulates plasminogen activator inhibitor type 2 (PAI-2) polymerizationPolymerization of plasminogen activator inhibitor-1.Altered native stability is the dominant basis for susceptibility of α1-antitrypsin mutants to polymerization.Three new alpha1-antitrypsin deficiency variants help to define a C-terminal region regulating conformational change and polymerization.The shapes of Z-α1-antitrypsin polymers in solution support the C-terminal domain-swap mechanism of polymerization.Local conformational flexibility provides a basis for facile polymer formation in human neuroserpinThe human serpin proteinase inhibitor-9 self-associates at physiological temperatures.alpha(1)-Proteinase inhibitor mutants with specificity for plasma kallikrein and C1s but not C1An antibody that prevents serpin polymerisation acts by inducing a novel allosteric behaviour.Probing serpin conformational change using mass spectrometry and related methods.An antibody raised against a pathogenic serpin variant induces mutant-like behaviour in the wild-type protein.Loop variants of the serpin thyroxine-binding globulin: implications for hormone release upon limited proteolysis.Molecular cloning of endopin 1, a novel serpin localized to neurosecretory vesicles of chromaffin cells. Inhibition of basic residue-cleaving proteases by endopin 1.The structural basis of serpin polymerization studied by hydrogen/deuterium exchange and mass spectrometry.Loop-sheet mechanism of serpin polymerization tested by reactive center loop mutations.Local and global effects of a cavity filling mutation in a metastable serpin.Effects of glycosylation on the stability and flexibility of a metastable protein: the human serpin α(1)-antitrypsin.Molecular contortionism - on the physical limits of serpin 'loop-sheet' polymers.Probing the local conformational change of alpha1-antitrypsin.Alpha-1-antitrypsin is present in the specific granules of human eosinophilic granulocytes.Probing the folding pathway of a consensus serpin using single tryptophan mutants.Probing the unfolding pathway of alpha1-antitrypsin.Pathogenic α1-Antitrypsin Polymers Are Formed by Reactive Loop-β-Sheet A LinkageA Kinetic Mechanism for the Polymerization of α1-Antitrypsin
P2860
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P2860
Importance of the release of strand 1C to the polymerization mechanism of inhibitory serpins
description
1997 nî lūn-bûn
@nan
1997 թուականի Յունուարին հրատարակուած գիտական յօդուած
@hyw
1997 թվականի հունվարին հրատարակված գիտական հոդված
@hy
1997年の論文
@ja
1997年論文
@yue
1997年論文
@zh-hant
1997年論文
@zh-hk
1997年論文
@zh-mo
1997年論文
@zh-tw
1997年论文
@wuu
name
Importance of the release of s ...... echanism of inhibitory serpins
@ast
Importance of the release of s ...... echanism of inhibitory serpins
@en
Importance of the release of s ...... echanism of inhibitory serpins
@nl
type
label
Importance of the release of s ...... echanism of inhibitory serpins
@ast
Importance of the release of s ...... echanism of inhibitory serpins
@en
Importance of the release of s ...... echanism of inhibitory serpins
@nl
prefLabel
Importance of the release of s ...... echanism of inhibitory serpins
@ast
Importance of the release of s ...... echanism of inhibitory serpins
@en
Importance of the release of s ...... echanism of inhibitory serpins
@nl
P2093
P2860
P3181
P356
P1433
P1476
Importance of the release of s ...... echanism of inhibitory serpins
@en
P2093
J Whisstock
M R Wardell
P C Hopkins
R W Carrell
P2860
P3181
P356
10.1002/PRO.5560060110
P407
P577
1997-01-01T00:00:00Z