INT309751

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Context Info
Confidence 0.08
First Reported 2010
Last Reported 2010
Negated 0
Speculated 0
Reported most in Body
Documents 1
Total Number 3
Disease Relevance 0
Pain Relevance 0.23

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

lyase activity (CA2) transmembrane transport (TRPV4) response to stress (CA2)
cytoplasm (CA2) cytosol (CA2) extracellular space (CA2)
CA2 (Homo sapiens)
TRPV4 (Homo sapiens)
Pain Link Frequency Relevance Heat
adenocard 3 89.48 High High
TRP channel 12 81.64 Quite High
agonist 9 77.60 Quite High
qutenza 3 45.48 Quite Low
addiction 6 5.00 Very Low Very Low Very Low
imagery 3 5.00 Very Low Very Low Very Low

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Sentences Mentioned In

Key: Protein Mutation Event Anatomy Negation Speculation Pain term Disease term
Using protein interaction experiments and functional assays, we show that the molecular correlate of Ca2+-dependent current potentiation is disruption of an interdomain interaction within TRPV4 resulting from CaM binding to a C-terminal site.
Ca2 Binding (interaction) of TRPV4
1) Confidence 0.08 Published 2010 Journal PLoS ONE Section Body Doc Link PMC2867956 Disease Relevance 0 Pain Relevance 0.07
The first comprises a ternary interaction in which Ca2+-loaded CaM binds to two different sites within the TRPV4 protein thus bringing two regulatory domains in proximity to each other.
Ca2 Binding (binds) of TRPV4 protein
2) Confidence 0.08 Published 2010 Journal PLoS ONE Section Body Doc Link PMC2867956 Disease Relevance 0 Pain Relevance 0.07
In contrast to these findings, TRPV4 neither binds to CaM in Ca2+-free buffers, nor to CaM1234, and potentiation of its activity directly depends on CaM interaction triggered by a rise in Ca2+.
Ca2 Binding (binds) of TRPV4
3) Confidence 0.07 Published 2010 Journal PLoS ONE Section Body Doc Link PMC2867956 Disease Relevance 0 Pain Relevance 0.09

General Comments

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