INT325899

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Context Info
Confidence 0.12
First Reported 2010
Last Reported 2010
Negated 0
Speculated 0
Reported most in Body
Documents 1
Total Number 6
Disease Relevance 2.43
Pain Relevance 0

This is a graph with borders and nodes. Maybe there is an Imagemap used so the nodes may be linking to some Pages.

pigmentation (Hps3) peptidase activity (F2) extracellular space (F2)
extracellular region (F2) cytoplasm (Hps3)
Anatomy Link Frequency
blood 1
Hps3 (Mus musculus)
F2 (Mus musculus)
Pain Link Frequency Relevance Heat
Inflammation 12 5.00 Very Low Very Low Very Low
Pain 6 5.00 Very Low Very Low Very Low
Arthritis 6 5.00 Very Low Very Low Very Low
Disease Link Frequency Relevance Heat
Coagulation Disorder 108 97.76 Very High Very High Very High
Abscess 378 96.32 Very High Very High Very High
Sprains And Strains 150 95.72 Very High Very High Very High
Bacteremia 60 92.92 High High
Sepsis 36 92.72 High High
Disease 78 89.04 High High
Immunization 54 51.04 Quite High
Yersinia Infection 6 26.88 Quite Low
Staphylococcus Infection 90 5.00 Very Low Very Low Very Low
Infection 90 5.00 Very Low Very Low Very Low

Sentences Mentioned In

Key: Protein Mutation Event Anatomy Negation Speculation Pain term Disease term
For the coagulase-prothrombin interaction, coagulase was injected at 10 pM, 0.1 nM, 1 nM, 5 nM, 10 nM, 25 nM, and 50 nM for 300 seconds followed by 300 seconds of dissociation followed by regeneration with NaOH (50 µL, 30 seconds).
coa Binding (interaction) of prothrombin
1) Confidence 0.12 Published 2010 Journal PLoS Pathogens Section Body Doc Link PMC2916881 Disease Relevance 0.05 Pain Relevance 0
Clinical isolates of the human pathogen Staphylococcus aureus secrete coagulase (Coa), a polypeptide that binds to and activates prothrombin, thereby converting fibrinogen to fibrin and promoting clotting of plasma or blood.
coa Binding (binds) of prothrombin in blood associated with coagulation disorder
2) Confidence 0.12 Published 2010 Journal PLoS Pathogens Section Abstract Doc Link PMC2916881 Disease Relevance 0.93 Pain Relevance 0
The KD for the coagulase·prothrombin interaction is lower than the reported affinity for the D1D2 domain alone [36]; we currently do not appreciate the basis for this difference.
coa Binding (interaction) of prothrombin
3) Confidence 0.12 Published 2010 Journal PLoS Pathogens Section Body Doc Link PMC2916881 Disease Relevance 0.25 Pain Relevance 0
For the coagulase-prothrombin interaction, coagulase was injected at 10 pM, 0.1 nM, 1 nM, 5 nM, 10 nM, 25 nM, and 50 nM for 300 seconds followed by 300 seconds of dissociation followed by regeneration with NaOH (50 µL, 30 seconds).
coa Binding (interaction) of prothrombin
4) Confidence 0.12 Published 2010 Journal PLoS Pathogens Section Body Doc Link PMC2916881 Disease Relevance 0.05 Pain Relevance 0
The KD for the coagulase·prothrombin interaction is lower than the reported affinity for the D1D2 domain alone [36]; we currently do not appreciate the basis for this difference.
coa Binding (interaction) of prothrombin
5) Confidence 0.12 Published 2010 Journal PLoS Pathogens Section Body Doc Link PMC2916881 Disease Relevance 0.25 Pain Relevance 0
Antibodies directed against Coa or vWbp prevent coagulase binding to prothrombin or fibrinogen and confer protection against challenge with S. aureus Newman or the methicillin-resistant S. aureus isolate USA300 LAC in mouse models of abscess formation or lethal sepsis.
coa Binding (binding) of prothrombin associated with abscess and sepsis
6) Confidence 0.12 Published 2010 Journal PLoS Pathogens Section Abstract Doc Link PMC2916881 Disease Relevance 0.90 Pain Relevance 0

General Comments

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