The acid stabilization of plasminogen activator inhibitor-1 depends on protonation of a single group that affects loop insertion into beta-sheet A.
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Structural Basis for Recognition of Urokinase-type Plasminogen Activator by Plasminogen Activator Inhibitor-1Polymerization of plasminogen activator inhibitor-1.Partitioning of serpin-proteinase reactions between stable inhibition and substrate cleavage is regulated by the rate of serpin reactive center loop insertion into beta-sheet A.Emerging anticoagulant and thrombolytic drugs.The molecular basis for anti-proteolytic and non-proteolytic functions of plasminogen activator inhibitor type-1: roles of the reactive centre loop, the shutter region, the flexible joint region and the small serpin fragment.Blocking formation of large protein aggregates by small peptides.Proteolytic regulation of epithelial sodium channels by urokinase plasminogen activator: cutting edge and cleavage sites.Mixture-based combinatorial libraries from small individual peptide libraries: a case study on α1-antitrypsin deficiency.New antithrombotic drugs: Antithrombotic Therapy and Prevention of Thrombosis, 9th ed: American College of Chest Physicians Evidence-Based Clinical Practice GuidelinesUrokinase links plasminogen activation and cell adhesion by cleavage of the RGD motif in vitronectin.Structural differences between active forms of plasminogen activator inhibitor type 1 revealed by conformationally sensitive ligands.The conversion of active to latent plasminogen activator inhibitor-1 is an energetically silent event.Loop variants of the serpin thyroxine-binding globulin: implications for hormone release upon limited proteolysis.The status of plasminogen activator inhibitor-1 as a therapeutic target.A peptide mimicking the C-terminal part of the reactive center loop induces the transition to the latent form of plasminogen activator inhibitor type-1.A regulatory hydrophobic area in the flexible joint region of plasminogen activator inhibitor-1, defined with fluorescent activity-neutralizing ligands. Ligand-induced serpin polymerization.Site-directed targeting of plasminogen activator inhibitor-1 as an example for a novel approach in rational drug design.Cloning and paratope analysis of an antibody fragment, a rational approach for the design of a PAI-1 inhibitor.Antithrombotic agents in the treatment of severe sepsis.Inhibition of plasminogen activator inhibitor-1: antibody fragments and their unique sequences as a tool for the development of profibrinolytic drugs.Functional stability of plasminogen activator inhibitor-1
P2860
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P2860
The acid stabilization of plasminogen activator inhibitor-1 depends on protonation of a single group that affects loop insertion into beta-sheet A.
description
1995 nî lūn-bûn
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1995年の論文
@ja
1995年学术文章
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1995年学术文章
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1995年学术文章
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1995年学术文章
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1995年学术文章
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1995年学术文章
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1995年學術文章
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1995年學術文章
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name
The acid stabilization of plas ...... p insertion into beta-sheet A.
@en
The acid stabilization of plas ...... p insertion into beta-sheet A.
@nl
type
label
The acid stabilization of plas ...... p insertion into beta-sheet A.
@en
The acid stabilization of plas ...... p insertion into beta-sheet A.
@nl
prefLabel
The acid stabilization of plas ...... p insertion into beta-sheet A.
@en
The acid stabilization of plas ...... p insertion into beta-sheet A.
@nl
P2860
P356
P1476
The acid stabilization of plas ...... p insertion into beta-sheet A.
@en
P2093
P2860
P304
27942-27947
P356
10.1074/JBC.270.46.27942
P407
P577
1995-11-01T00:00:00Z