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

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

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

http://www.wikidata.org/entity/Q27642265

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Fibrinogen substrate recognition by staphylocoagulase.(pro)thrombin complexes Novel fluorescent prothrombin analogs as probes of staphylocoagulase-prothrombin interactions Proteolytic inactivation of tissue factor pathway inhibitor by bacterial omptins Optical imaging of bacterial infections Staphylococcal manipulation of host immune responses Endocarditis and molecular imaging Staphylococcus aureus secretes coagulase and von Willebrand factor binding protein to modify the coagulation cascade and establish host infections Contribution of coagulases towards Staphylococcus aureus disease and protective immunity Two distinct coagulase-dependent barriers protect Staphylococcus aureus from neutrophils in a three dimensional in vitro infection model Crystal structure of prethrombin-1 Structural basis of thrombin-mediated factor V activation: the Glu666-Glu672 sequence is critical for processing at the heavy chain-B domain junction Crystal Structures of Prethrombin-2 Reveal Alternative Conformations under Identical Solution Conditions and the Mechanism of Zymogen Activation Crystal Structure of Prothrombin Reveals Conformational Flexibility and Mechanism of Activation Exposure of R169 controls protein C activation and autoactivation Rezymogenation of active urokinase induced by an inhibitory antibody An allosteric switch for pro-HGF/Met signaling using zymogen activator peptides Pathogenesis of Staphylococcus aureus abscesses Homology Modeling of Coagulase in Staphylococcus aureus The staphylocoagulase family of zymogen activator and adhesion proteins.Genetic diversity of staphylocoagulase genes (coa): insight into the evolution of variable chromosomal virulence factors in Staphylococcus aureus Global transcriptome responses including small RNAs during mixed-species interactions with methicillin-resistant Staphylococcus aureus and Pseudomonas aeruginosa A revisit to the one form kinetic model of prothrombinase Ratcheting of the substrate from the zymogen to proteinase conformations directs the sequential cleavage of prothrombin by prothrombinase.Preventing Staphylococcus aureus sepsis through the inhibition of its agglutination in blood.Rapid binding of plasminogen to streptokinase in a catalytic complex reveals a three-step mechanism.Vaccine protection of leukopenic mice against Staphylococcus aureus bloodstream infection A play in four acts: Staphylococcus aureus abscess formation Engineering streptokinase for generation of active site-labeled plasminogen analogs.In vivo detection of Staphylococcus aureus endocarditis by targeting pathogen-specific prothrombin activation Prolylcarboxypeptidase independently activates plasma prekallikrein (fletcher factor).Allostery in trypsin-like proteases suggests new therapeutic strategies.Utilizing the activation mechanism of serine proteases to engineer hepatocyte growth factor into a Met antagonist Pathogen activators of plasminogen Complete genome of Staphylococcus aureus Tager 104 provides evidence of its relation to modern systemic hospital-acquired strains.Contribution of Staphylococcus aureus Coagulases and Clumping Factor A to Abscess Formation in a Rabbit Model of Skin and Soft Tissue Infection.The structure of thrombin, a chameleon-like proteinase.Conformational selection in trypsin-like proteases.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.

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P2860

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

http://www.wikidata.org/entity/Q27642265

description

2003 nî lūn-bûn

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2003 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած

@hyw

2003 թվականի հոտեմբերին հրատարակված գիտական հոդված

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2003年の論文

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2003年論文

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2003年論文

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2003年論文

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2003年論文

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2003年論文

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2003年论文

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name

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

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

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

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type

label

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

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

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

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prefLabel

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

@ast

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

@en

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

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

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Pablo Fuentes-Prior

http://www.w3.org/2001/XMLSchema#string

Patricia J Anderson

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Rainer Friedrich

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Robert Huber

http://www.w3.org/2001/XMLSchema#string

Shun-Ichiro Kawabata

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P2860

Complete genome sequence and comparative genomic analysis of an emerging human pathogen, serotype V Streptococcus agalactiae.

Genome sequence of Streptococcus agalactiae, a pathogen causing invasive neonatal disease

Molecular mechanisms for the conversion of zymogens to active proteolytic enzymes

Pathogenic bacteria attach to human fibronectin through a tandem beta-zipper

Crystal structure of the catalytic domain of human plasmin complexed with streptokinase

The ternary microplasmin-staphylokinase-microplasmin complex is a proteinase-cofactor-substrate complex in action

A novel von Willebrand factor binding protein expressed by Staphylococcus aureus.

Role of fibronectin-binding MSCRAMMs in bacterial adherence and entry into mammalian cells.

Deletion of Ile1 changes the mechanism of streptokinase: evidence for the molecular sexuality hypothesis.

Infective endocarditis in adults.

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535-9

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scholarly article

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545055

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10.1038/NATURE01962

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6957

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425

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Ingrid M. Verhamme

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2003-10-02T00:00:00Z

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9069221

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1016967838

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14523451

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