INT118489

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Context Info
Confidence 0.57
First Reported 2004
Last Reported 2008
Negated 0
Speculated 0
Reported most in Abstract
Documents 4
Total Number 4
Disease Relevance 0
Pain Relevance 0.37

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

cytosol (TRPV1) transport (TRPV1) plasma membrane (TRPV1)
lipid metabolic process (TRPV1)
Anatomy Link Frequency
pore 2
TRPV1 (Homo sapiens)
Pain Link Frequency Relevance Heat
bradykinin 1 90.96 High High
TRP channel 6 76.28 Quite High
vanilloid receptor subtype 1 2 75.00 Quite High
qutenza 13 70.48 Quite High
Nerve growth factor 1 49.04 Quite Low
Inflammation 4 42.16 Quite Low
diabetic neuropathy 1 34.16 Quite Low
addiction 19 25.76 Quite Low
Pain 2 25.00 Low Low
Hyperalgesia 2 25.00 Low Low
Disease Link Frequency Relevance Heat
INFLAMMATION 2 42.16 Quite Low
Nervous System Injury 1 37.12 Quite Low
Diabetic Neuropathy 1 34.16 Quite Low
Hyperalgesia 2 25.00 Low Low
Functional Bowel Disorder 1 25.00 Low Low
Disease 1 25.00 Low Low
Neuropathic Pain 1 25.00 Low Low
Inflammatory Bowel Disease 1 25.00 Low Low
Bacillus Anthracis Infection 2 5.00 Very Low Very Low Very Low
Pain 1 5.00 Very Low Very Low Very Low

Sentences Mentioned In

Key: Protein Mutation Event Anatomy Negation Speculation Pain term Disease term
Yeast two-hybrid and pull-down assays showed that self-association of the TRPV1-C is blocked when segment 684Glu-721Arg is deleted.
Negative_regulation (blocked) of TRPV1 Binding (association) of
1) Confidence 0.57 Published 2004 Journal J. Neurosci. Section Abstract Doc Link 15190102 Disease Relevance 0 Pain Relevance 0.11
The second level of control is by forming TRPV1 heteromers and their association with putative regulatory proteins.
Negative_regulation (forming) of TRPV1 Binding (association) of
2) Confidence 0.43 Published 2004 Journal Eur. J. Biochem. Section Abstract Doc Link 15128291 Disease Relevance 0 Pain Relevance 0.15
Biochemical and immunological analysis indicate that removal of the AD from full-length TRPV1 monomers blocks the formation of stable heteromeric assemblies with wild-type TRPV1 subunits.
Negative_regulation (blocks) of TRPV1 Binding (assemblies) of
3) Confidence 0.36 Published 2004 Journal J. Neurosci. Section Abstract Doc Link 15190102 Disease Relevance 0 Pain Relevance 0.10
This interaction with Na+ also suggests that QA blockers bind to an intracellular site in the pore of TRPV1 channels, allowing us to use these molecules as probes for obtaining information about the pore properties of this channel protein.


Negative_regulation (blockers) of TRPV1 Binding (bind) of in pore
4) Confidence 0.16 Published 2008 Journal The Journal of General Physiology Section Body Doc Link PMC2571972 Disease Relevance 0 Pain Relevance 0

General Comments

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