INT276964

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Context Info
Confidence 0.24
First Reported 2009
Last Reported 2010
Negated 0
Speculated 0
Reported most in Body
Documents 11
Total Number 11
Disease Relevance 4.22
Pain Relevance 0.89

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 (Tlr1, Tlr2) plasma membrane (Tlr1, Tlr2) intracellular (Tlr1, Tlr2)
cytoplasm (Tlr2)
Tlr1 (Mus musculus)
Tlr2 (Mus musculus)
Pain Link Frequency Relevance Heat
Inflammation 93 95.68 Very High Very High Very High
agonist 39 93.16 High High
cytokine 91 92.68 High High
tolerance 36 65.32 Quite High
Inflammatory response 49 64.28 Quite High
ischemia 44 58.64 Quite High
chemokine 19 40.52 Quite Low
fibrosis 4 33.36 Quite Low
Central nervous system 42 20.08 Low Low
addiction 3 19.96 Low Low
Disease Link Frequency Relevance Heat
Injury 125 99.32 Very High Very High Very High
Lyme Disease 13 99.10 Very High Very High Very High
INFLAMMATION 126 95.68 Very High Very High Very High
American Trypanosomiasis 2 94.72 High High
Hemorrhagic Shock 66 91.76 High High
Bacterial Respiratory Disease 7 86.24 High High
Infection 56 82.04 Quite High
Systemic Lupus Erythematosus 85 68.16 Quite High
Cancer 174 66.44 Quite High
Apoptosis 105 62.00 Quite High

Sentences Mentioned In

Key: Protein Mutation Event Anatomy Negation Speculation Pain term Disease term
Finally, TLR2 heterodimerizes with TLR1 and TLR6, and TLR2 signaling is modulated by other non-TLR receptors such as dectin-1 [47], asioloGM1 [48], and CXCR4 [49].
TLR1 Binding (heterodimerizes) of TLR2
1) Confidence 0.24 Published 2010 Journal PLoS ONE Section Body Doc Link PMC2816997 Disease Relevance 0.48 Pain Relevance 0.16
Finally, TLR2 heterodimerizes with TLR1 and TLR6, and TLR2 signaling is modulated by other non-TLR receptors such as dectin-1 [47], asioloGM1 [48], and CXCR4 [49].
TLR1 Binding (heterodimerizes) of TLR2
2) Confidence 0.24 Published 2010 Journal PLoS ONE Section Body Doc Link PMC2816997 Disease Relevance 0.47 Pain Relevance 0.17
Since TLR2 functions via dimerization with TLR1, TLR6, or Dectin-1, respectively [15], we examined the dimerizing partners of TLR2 in these cells and found that TLR2 co-localized with TLR6 or Dectin-1, but not TLR1 (Fig. 1C).
TLR1 Binding (dimerization) of TLR2
3) Confidence 0.22 Published 2009 Journal PLoS ONE Section Body Doc Link PMC2716531 Disease Relevance 0.30 Pain Relevance 0.08
Since TLR2 functions via dimerization with TLR1, TLR6, or Dectin-1, respectively [15], we examined the dimerizing partners of TLR2 in these cells and found that TLR2 co-localized with TLR6 or Dectin-1, but not TLR1 (Fig. 1C).
TLR1 Binding (localized) of TLR2
4) Confidence 0.19 Published 2009 Journal PLoS ONE Section Body Doc Link PMC2716531 Disease Relevance 0.28 Pain Relevance 0.07
TLR2 can form a complex with TLR1 or TLR6 and respond to lipopeptides from a wide variety of microbes.
TLR1 Binding (form) of TLR2
5) Confidence 0.14 Published 2010 Journal Mediators of Inflammation Section Body Doc Link PMC2913815 Disease Relevance 0.13 Pain Relevance 0.07
TLR2 can form a complex with TLR1 or TLR6 and respond to lipopeptides from a wide variety of microbes.
TLR1 Binding (complex) of TLR2
6) Confidence 0.14 Published 2010 Journal Mediators of Inflammation Section Body Doc Link PMC2913815 Disease Relevance 0.13 Pain Relevance 0.07
Briefly, TLR2, which works with TLR1 or TLR6, recognizes bacterial components, such as lipopeptide and lipoprotein of gram-positive bacteria; specifically, the heterodimer TLR1/2 which can recognize triacyl lipopeptide, while TLR2/6 recognizes diacyl lipopeptide.TLR7 is documented to recognize RNA, while TLR9-DNA, both microbial and self [89, 90].


TLR1 Binding (works) of TLR2
7) Confidence 0.08 Published 2010 Journal Autoimmune Diseases Section Body Doc Link PMC2989704 Disease Relevance 0.18 Pain Relevance 0.03
The resulting TLR1/TLR2 and TLR6/TLR2 complexes recognize distinct ligands, triacyl and diacyl lipoproteins, respectively.
TLR1 Binding (complexes) of TLR2
8) Confidence 0.08 Published 2010 Journal Mediators of Inflammation Section Body Doc Link PMC2913855 Disease Relevance 0.79 Pain Relevance 0.05
TLR2 recognizes its ligands by forming a heterodimer with either TLR1 or TLR6.
TLR1 Binding (recognizes) of TLR2
9) Confidence 0.07 Published 2010 Journal Mediators of Inflammation Section Body Doc Link PMC2913855 Disease Relevance 0.81 Pain Relevance 0.06
The principal proinflammatory DAMPs of the spirochetal pathogen Borrelia burgdorferi, the causative agent of Lyme disease, are triacylated lipoproteins recognized by heterodimers of TLR2 and TLR1 [1].
TLR1 Binding (heterodimers) of TLR2 associated with lyme disease
10) Confidence 0.05 Published 2009 Journal PLoS Pathogens Section Body Doc Link PMC2781632 Disease Relevance 0.57 Pain Relevance 0.13
TLR2 can form heterodimers with TLR1 and TLR6, thereby improving the recognition of the target lipoteichoic acids [63].
TLR1 Binding (heterodimers) of TLR2
11) Confidence 0.02 Published 2010 Journal International Journal of Inflammation Section Body Doc Link PMC3003996 Disease Relevance 0.09 Pain Relevance 0

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