Fibrinogen substrate recognition by staphylocoagulase.(pro)thrombin complexes - Test2 - elhamkhani - TriplyDB

Fibrinogen substrate recognition by staphylocoagulase.(pro)thrombin complexes

Fibrinogen substrate recognition by staphylocoagulase.(pro)thrombin complexes

http://www.wikidata.org/entity/Q24338455

about

Novel fluorescent prothrombin analogs as probes of staphylocoagulase-prothrombin interactions Optical imaging of bacterial infections Staphylococcal manipulation of host immune responses Contribution of coagulases towards Staphylococcus aureus disease and protective immunity Homology Modeling of Coagulase in Staphylococcus aureus Preventing Staphylococcus aureus sepsis through the inhibition of its agglutination in blood.Positive selection during the evolution of the blood coagulation factors in the context of their disease-causing mutations.Global analysis of community-associated methicillin-resistant Staphylococcus aureus exoproteins reveals molecules produced in vitro and during infection.Igniting the fire: Staphylococcus aureus virulence factors in the pathogenesis of sepsis.In vivo detection of Staphylococcus aureus endocarditis by targeting pathogen-specific prothrombin activation Complete genome of Staphylococcus aureus Tager 104 provides evidence of its relation to modern systemic hospital-acquired strains.Coagulases as determinants of protective immune responses against Staphylococcus aureus.Effect of zymogen domains and active site occupation on activation of prothrombin by von Willebrand factor-binding protein.Coagulase and Efb of Staphylococcus aureus Have a Common Fibrinogen Binding Motif.Exploring Staphylococcus aureus pathways to disease for vaccine development.Structural basis for reduced staphylocoagulase-mediated bovine prothrombin activation Genetic elimination of the binding motif on fibrinogen for the S. aureus virulence factor ClfA improves host survival in septicemia.Von Willebrand factor-binding protein is a hysteretic conformational activator of prothrombin Pathogenesis of Staphylococcus aureus Bloodstream Infections.Fibrinogen Is at the Interface of Host Defense and Pathogen Virulence in Staphylococcus aureus Infection.Staphylococcus aureus Manipulates Innate Immunity through Own and Host-Expressed Proteases Staphylococcus aureus: the current state of disease, pathophysiology and strategies for prevention.RGD delivery of truncated coagulase to tumor vasculature affords local thrombotic activity to induce infarction of tumors in mice.Thrombin-activatable fibrinolysis inhibitor binds to Streptococcus pyogenes by interacting with collagen-like proteins A and B.NGR (Asn-Gly-Arg)-targeted delivery of coagulase to tumor vasculature arrests cancer cell growth.

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P2860

Fibrinogen substrate recognition by staphylocoagulase.(pro)thrombin complexes

http://www.wikidata.org/entity/Q24338455

description

2006 nî lūn-bûn

@nan

2006 թուականի Յունուարին հրատարակուած գիտական յօդուած

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2006 թվականի հունվարին հրատարակված գիտական հոդված

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2006年の論文

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2006年論文

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2006年論文

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2006年論文

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2006年論文

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2006年論文

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2006年论文

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name

Fibrinogen substrate recognition by staphylocoagulase.(pro)thrombin complexes

@ast

Fibrinogen substrate recognition by staphylocoagulase.(pro)thrombin complexes

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Fibrinogen substrate recognition by staphylocoagulase.(pro)thrombin complexes

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Fibrinogen substrate recognition by staphylocoagulase.(pro)thrombin complexes

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type

label

Fibrinogen substrate recognition by staphylocoagulase.(pro)thrombin complexes

@ast

Fibrinogen substrate recognition by staphylocoagulase.(pro)thrombin complexes

@en

Fibrinogen substrate recognition by staphylocoagulase.(pro)thrombin complexes

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Fibrinogen substrate recognition by staphylocoagulase.(pro)thrombin complexes

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prefLabel

Fibrinogen substrate recognition by staphylocoagulase.(pro)thrombin complexes

@ast

Fibrinogen substrate recognition by staphylocoagulase.(pro)thrombin complexes

@en

Fibrinogen substrate recognition by staphylocoagulase.(pro)thrombin complexes

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Fibrinogen substrate recognition by staphylocoagulase.(pro)thrombin complexes

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Journal of Biological Chemistry

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Fibrinogen substrate recognition by staphylocoagulase.(pro)thrombin complexes

@en

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Pablo Fuentes-Prior

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Rainer Friedrich

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P2860

Complete genomes of two clinical Staphylococcus aureus strains: evidence for the rapid evolution of virulence and drug resistance

CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice

Novel fluorescent prothrombin analogs as probes of staphylocoagulase-prothrombin interactions

The Protein Data Bank

Molecular mechanisms for the conversion of zymogens to active proteolytic enzymes

The crystal structure of modified bovine fibrinogen

Structural basis for the anticoagulant activity of the thrombin-thrombomodulin complex

Crystal structure of the central region of bovine fibrinogen (E5 fragment) at 1.4-A resolution

Crystal structure of native chicken fibrinogen at 2.7 A resolution

Staphylocoagulase is a prototype for the mechanism of cofactor-induced zymogen activation

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1179-87

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scholarly article

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1848108

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10.1074/JBC.M507956200

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2

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281

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