Novel fluorescent prothrombin analogs as probes of staphylocoagulase-prothrombin interactions
about
Fibrinogen substrate recognition by staphylocoagulase.(pro)thrombin complexesEndocarditis and molecular imagingActive site-labeled prothrombin inhibits prothrombinase in vitro and thrombosis in vivo.A compact water-soluble porphyrin bearing an iodoacetamido bioconjugatable site.Spatial distribution of factor Xa, thrombin, and fibrin(ogen) on thrombi at venous shearInhibition of thrombin formation by active site mutated (S360A) activated protein C.Rapid binding of plasminogen to streptokinase in a catalytic complex reveals a three-step mechanism.Engineering streptokinase for generation of active site-labeled plasminogen analogs.In vivo detection of Staphylococcus aureus endocarditis by targeting pathogen-specific prothrombin activationNotecarin D binds human factor V and factor Va with high affinity in the absence of membranes.Complete genome of Staphylococcus aureus Tager 104 provides evidence of its relation to modern systemic hospital-acquired strains.Effect of zymogen domains and active site occupation on activation of prothrombin by von Willebrand factor-binding protein.Exploring Staphylococcus aureus pathways to disease for vaccine development.Restricted active site docking by enzyme-bound substrate enforces the ordered cleavage of prothrombin by prothrombinase.Structural basis for reduced staphylocoagulase-mediated bovine prothrombin activationMolecular imaging of bacterial infections in vivo: the discrimination of infection from inflammation.Exosites in the substrate specificity of blood coagulation reactions.Von Willebrand factor-binding protein is a hysteretic conformational activator of prothrombinSmall-molecule modulators of zymogen activation in the fibrinolytic and coagulation systems.HD1, a thrombin-directed aptamer, binds exosite 1 on prothrombin with high affinity and inhibits its activation by prothrombinase.Development of coagulation factor probes for the identification of procoagulant circulating tumor cells.A novel mode of intervention with serine protease activity: targeting zymogen activation.
P2860
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P2860
Novel fluorescent prothrombin analogs as probes of staphylocoagulase-prothrombin interactions
description
2006 nî lūn-bûn
@nan
2006 թուականի Յունուարին հրատարակուած գիտական յօդուած
@hyw
2006 թվականի հունվարին հրատարակված գիտական հոդված
@hy
2006年の論文
@ja
2006年論文
@yue
2006年論文
@zh-hant
2006年論文
@zh-hk
2006年論文
@zh-mo
2006年論文
@zh-tw
2006年论文
@wuu
name
Novel fluorescent prothrombin ...... ulase-prothrombin interactions
@ast
Novel fluorescent prothrombin ...... ulase-prothrombin interactions
@en
Novel fluorescent prothrombin ...... ulase-prothrombin interactions
@en-gb
Novel fluorescent prothrombin ...... ulase-prothrombin interactions
@nl
type
label
Novel fluorescent prothrombin ...... ulase-prothrombin interactions
@ast
Novel fluorescent prothrombin ...... ulase-prothrombin interactions
@en
Novel fluorescent prothrombin ...... ulase-prothrombin interactions
@en-gb
Novel fluorescent prothrombin ...... ulase-prothrombin interactions
@nl
prefLabel
Novel fluorescent prothrombin ...... ulase-prothrombin interactions
@ast
Novel fluorescent prothrombin ...... ulase-prothrombin interactions
@en
Novel fluorescent prothrombin ...... ulase-prothrombin interactions
@en-gb
Novel fluorescent prothrombin ...... ulase-prothrombin interactions
@nl
P2093
P2860
P356
P1476
Novel fluorescent prothrombin ...... ulase-prothrombin interactions
@en
P2093
Guido Tans
Heather K Kroh
Judy Briggs
Pablo Fuentes-Prior
Peter Panizzi
Rainer Friedrich
P2860
P304
P356
10.1074/JBC.M507955200
P407
P577
2006-01-13T00:00:00Z