INT195160

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Context Info
Confidence 0.24
First Reported 2006
Last Reported 2010
Negated 0
Speculated 0
Reported most in Body
Documents 8
Total Number 11
Disease Relevance 5.83
Pain Relevance 0.53

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

signal transduction (TLR5) plasma membrane (TLR5) intracellular (TLR5)
Anatomy Link Frequency
epithelial cells 2
TLR5 (Homo sapiens)
TLR5 - F616L (2)
Pain Link Frequency Relevance Heat
Inflammatory response 31 98.36 Very High Very High Very High
Inflammation 34 89.44 High High
cytokine 35 88.40 High High
chemokine 3 57.08 Quite High
Inflammatory marker 2 50.36 Quite High
Arthritis 4 44.48 Quite Low
Pain 20 33.08 Quite Low
cva 4 24.00 Low Low
Bile 24 5.00 Very Low Very Low Very Low
tolerance 18 5.00 Very Low Very Low Very Low
Disease Link Frequency Relevance Heat
Infection 206 100.00 Very High Very High Very High
INFLAMMATION 49 98.00 Very High Very High Very High
Adhesions 16 90.60 High High
Syndrome 90 87.68 High High
Necrosis 6 87.28 High High
Cancer 6 86.92 High High
Thrombophilia 8 85.44 High High
Sprains And Strains 107 85.24 High High
Diarrhoea 106 78.68 Quite High
Abscess 12 73.92 Quite High

Sentences Mentioned In

Key: Protein Mutation Event Anatomy Negation Speculation Pain term Disease term
Stimulation with specific ligands targeted to the TLR1/2 heterodimer, TLR3, and TLR5 for the cultured limbal and conjunctival epithelial cells showed an increase in NF?
TLR5 Binding (heterodimer) of in epithelial cells
1) Confidence 0.24 Published 2007 Journal Molecular Vision Section Body Doc Link PMC2768757 Disease Relevance 0.14 Pain Relevance 0.07
The TLR5-F616L and TLR5-R392 mutations, which are associated with infections by flagellate bacteria, such as Legionella pneumophila [6], may also be associated with Fusobacterium necrophorum infections.
TLR5 (F616L) Binding (associated) of associated with infection
2) Confidence 0.16 Published 2006 Journal BMC Infect Dis Section Body Doc Link PMC1538604 Disease Relevance 0.79 Pain Relevance 0
The TLR5-F616L and TLR5-R392 mutations, which are associated with infections by flagellate bacteria, such as Legionella pneumophila [6], may also be associated with Fusobacterium necrophorum infections.
TLR5 (F616L) Binding (associated) of associated with infection
3) Confidence 0.16 Published 2006 Journal BMC Infect Dis Section Body Doc Link PMC1538604 Disease Relevance 0.83 Pain Relevance 0
The TLR5-F616L and TLR5-R392 mutations, which are associated with infections by flagellate bacteria, such as Legionella pneumophila [6], may also be associated with Fusobacterium necrophorum infections.
TLR5 Binding (associated) of associated with infection
4) Confidence 0.16 Published 2006 Journal BMC Infect Dis Section Body Doc Link PMC1538604 Disease Relevance 0.79 Pain Relevance 0
The TLR5-F616L and TLR5-R392 mutations, which are associated with infections by flagellate bacteria, such as Legionella pneumophila [6], may also be associated with Fusobacterium necrophorum infections.
TLR5 Binding (associated) of associated with infection
5) Confidence 0.16 Published 2006 Journal BMC Infect Dis Section Body Doc Link PMC1538604 Disease Relevance 0.83 Pain Relevance 0
These cellular responses are primarily mediated by flagellin (fliC), a major bacterial surface protein of EAEC [28], whichcauses IL-8 release by binding to Toll-like receptor 5 (TLR5).
Toll-like receptor 5 Binding (binding) of
6) Confidence 0.15 Published 2010 Journal Interdisciplinary Perspectives on Infectious Diseases Section Body Doc Link PMC2837894 Disease Relevance 0.76 Pain Relevance 0.18
These cellular responses are primarily mediated by flagellin (fliC), a major bacterial surface protein of EAEC [28], whichcauses IL-8 release by binding to Toll-like receptor 5 (TLR5).
TLR5 Binding (binding) of
7) Confidence 0.15 Published 2010 Journal Interdisciplinary Perspectives on Infectious Diseases Section Body Doc Link PMC2837894 Disease Relevance 0.76 Pain Relevance 0.18
This correlates with the observed protective effects of TLR5 signaling in epithelial homeostasis and may suggest that under physiological conditions flagellin ligation of TLR5 located on the apical surface of IECs does not exert an inflammatory response.
TLR5 Binding (ligation) of associated with inflammatory response
8) Confidence 0.12 Published 2010 Journal International Journal of Inflammation Section Body Doc Link PMC3003996 Disease Relevance 0.30 Pain Relevance 0.05
Toll-like receptor 5 (TLR5) can bind to a protein motif common to the flagellin protein making up the flagella from many bacteria, such as L. monocytogenes.
TLR5 Binding (bind) of
9) Confidence 0.12 Published 2010 Journal International Journal of Inflammation Section Body Doc Link PMC3003996 Disease Relevance 0.15 Pain Relevance 0
Toll-like receptor 5 (TLR5) can bind to a protein motif common to the flagellin protein making up the flagella from many bacteria, such as L. monocytogenes.
Toll-like receptor 5 Binding (bind) of
10) Confidence 0.12 Published 2010 Journal International Journal of Inflammation Section Body Doc Link PMC3003996 Disease Relevance 0.16 Pain Relevance 0
In contrast, flagellated bacteria that interact with basolateral TLR5 signal an invasion of the epithelium by bacteria, and therefore induce a strong proinflammatory response [7].
TLR5 Binding (interact) of in epithelium
11) Confidence 0.11 Published 2010 Journal International Journal of Inflammation Section Body Doc Link PMC3003996 Disease Relevance 0.32 Pain Relevance 0.05

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