INT208980

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Context Info
Confidence 0.32
First Reported 2007
Last Reported 2009
Negated 1
Speculated 0
Reported most in Body
Documents 4
Total Number 5
Disease Relevance 0.67
Pain Relevance 1.55

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

cytosol (Ca2, Trpv1) extracellular space (Ca2) lyase activity (Ca2)
plasma membrane (Trpv1) lipid metabolic process (Trpv1) response to stress (Ca2)
Anatomy Link Frequency
pore 1
Ca2 (Rattus norvegicus)
Trpv1 (Rattus norvegicus)
Pain Link Frequency Relevance Heat
qutenza 225 95.16 Very High Very High Very High
Pain 84 86.60 High High
antagonist 76 82.08 Quite High
TRP channel 18 72.00 Quite High
Endep 30 63.28 Quite High
antidepressant 6 61.44 Quite High
carbamazepine 6 54.24 Quite High
backache 3 48.16 Quite Low
nociceptor 9 38.40 Quite Low
agonist 21 30.48 Quite Low
Disease Link Frequency Relevance Heat
Pain 81 86.60 High High
Acidosis 282 72.00 Quite High
Hypoxia 124 50.00 Quite Low
Low Back Pain 3 48.80 Quite Low
Nociception 26 9.76 Low Low
Hyperalgesia 6 7.88 Low Low
Cv Unclassified Under Development 36 5.00 Very Low Very Low Very Low
Inflammatory Pain 15 5.00 Very Low Very Low Very Low
Acid Base Imbalance 10 5.00 Very Low Very Low Very Low
Lactic Acidosis 10 5.00 Very Low Very Low Very Low

Sentences Mentioned In

Key: Protein Mutation Event Anatomy Negation Speculation Pain term Disease term
In summary, Ni2+ blocks voltage-gated Ca2+ and Mn2+ entry, but not Ca2+ or Mn2+ influx through TRPV1.
Ca2 Neg (not) Binding (voltage) of TRPV1
1) Confidence 0.32 Published 2009 Journal Pflugers Arch Section Body Doc Link PMC2765625 Disease Relevance 0.26 Pain Relevance 0.36
In summary, Ni2+ blocks voltage-gated Ca2+ and Mn2+ entry, but not Ca2+ or Mn2+ influx through TRPV1.
Ca2 Binding (voltage) of TRPV1
2) Confidence 0.32 Published 2009 Journal Pflugers Arch Section Body Doc Link PMC2765625 Disease Relevance 0.26 Pain Relevance 0.36
Classical antipsychotic drugs, calmidazolium and camstatin may interact with TRPV1 on folds common in these Ca2+-binding proteins (i.e., at the Ca2+-filter/binding region).
Ca2 Binding (interact) of TRPV1
3) Confidence 0.17 Published 2007 Journal PLoS ONE Section Body Doc Link PMC1890308 Disease Relevance 0.15 Pain Relevance 0.22
Prompt inhibition of inducible Ca2+-uptake suggested a rapid interaction with a potential extracellular docking site(s) of TRPV1 (Fig. 4).
Ca2 Binding (interaction) of TRPV1
4) Confidence 0.17 Published 2007 Journal PLoS ONE Section Body Doc Link PMC1890308 Disease Relevance 0 Pain Relevance 0.54
This particular domain of the pore loop may also serve as a cation filter and anti-calmodulin compounds can bind after Ca2+ binds first to this TRPV1 structure (Fig. 10), thereby preventing pore opening [44], [45].
Ca2 Binding (binds) of TRPV1 in pore
5) Confidence 0.14 Published 2007 Journal PLoS ONE Section Body Doc Link PMC1890308 Disease Relevance 0 Pain Relevance 0.07

General Comments

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