Human plasminogen catalytic domain undergoes an unusual conformational change upon activation
about
The crystal structure of the zymogen catalytic domain of complement protease C1r reveals that a disruptive mechanical stress is required to trigger activation of the C1 complex.Crystal Structures of Prethrombin-2 Reveal Alternative Conformations under Identical Solution Conditions and the Mechanism of Zymogen ActivationThe structure of Human Microplasmin in Complex with Textilinin-1, an Aprotinin-like Inhibitor from the Australian Brown SnakeA 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.Analysis on conservation of disulphide bonds and their structural features in homologous protein domain familiesReduction of canine plasminogen leads to an expanded molecule which precipitates.Photonic activation of plasminogen induced by low dose UVB.Allostery in trypsin-like proteases suggests new therapeutic strategies.Conformational selection in trypsin-like proteases.Bacterial plasminogen receptors utilize host plasminogen system for effective invasion and dissemination.The plasmin-antiplasmin system: structural and functional aspects.Natural and engineered plasmin inhibitors: applications and design strategies.Molecular modelling, docking and interaction studies of human-plasmogen and salmonella enolase with enolase inhibitors.Over-expression and purification of active serine proteases and their variants from Escherichia coli inclusion bodies.Identification through combinatorial random and rational mutagenesis of a substrate-interacting exosite in the gamma domain of streptokinase.Purification and characterization of mutant miniPlasmin for thrombolytic therapy.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.A kringle-containing protease with plasminogen-like activity in the basal chordate Branchiostoma belcheri.Serine protease inhibitors to treat inflammation: a patent review (2011-2016).The mechanism of a bacterial plasminogen activator intermediate between streptokinase and staphylokinase.Domain truncation studies reveal that the streptokinase-plasmin activator complex utilizes long range protein-protein interactions with macromolecular substrate to maximize catalytic turnover.
P2860
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P2860
Human plasminogen catalytic domain undergoes an unusual conformational change upon activation
description
2000 nî lūn-bûn
@nan
2000 թուականի Յունուարին հրատարակուած գիտական յօդուած
@hyw
2000 թվականի հունվարին հրատարակված գիտական հոդված
@hy
2000年の論文
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2000年論文
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2000年論文
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2000年論文
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2000年論文
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2000年論文
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2000年论文
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name
Human plasminogen catalytic do ...... ational change upon activation
@ast
Human plasminogen catalytic do ...... ational change upon activation
@en
Human plasminogen catalytic do ...... ational change upon activation
@nl
type
label
Human plasminogen catalytic do ...... ational change upon activation
@ast
Human plasminogen catalytic do ...... ational change upon activation
@en
Human plasminogen catalytic do ...... ational change upon activation
@nl
prefLabel
Human plasminogen catalytic do ...... ational change upon activation
@ast
Human plasminogen catalytic do ...... ational change upon activation
@en
Human plasminogen catalytic do ...... ational change upon activation
@nl
P2093
P356
P1476
Human plasminogen catalytic do ...... ational change upon activation
@en
P2093
P304
P356
10.1006/JMBI.1999.3397
P407
P577
2000-01-28T00:00:00Z