INT309743

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Context Info
Confidence 0.04
First Reported 2010
Last Reported 2010
Negated 0
Speculated 0
Reported most in Body
Documents 1
Total Number 3
Disease Relevance 0
Pain Relevance 0.13

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

cytoplasm (CA2, CALM3) cytosol (CA2, CALM3) nucleoplasm (CALM3)
small molecule metabolic process (CALM3) lyase activity (CA2) carbohydrate metabolic process (CALM3)
CA2 (Homo sapiens)
CALM3 (Homo sapiens)
Pain Link Frequency Relevance Heat
adenocard 3 93.60 High High
TRP channel 12 85.76 High High
agonist 9 13.56 Low Low
addiction 6 5.00 Very Low Very Low Very Low
imagery 3 5.00 Very Low Very Low Very Low
qutenza 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 different experimental strategies, we have demonstrated that an interaction between an N-terminal and a C-terminal site in TRPV4 is present at nanomolar Ca2+ concentrations (Fig. 8A), but becomes disrupted secondary to CaM binding to the TRPV4 C terminus at micromolar Ca2+ concentrations (Fig. 8B).
Ca2 Binding (binding) of CaM
1) Confidence 0.04 Published 2010 Journal PLoS ONE Section Body Doc Link PMC2867956 Disease Relevance 0 Pain Relevance 0
For TRPM2, co-immunoprecipitation experiments demonstrated CaM1234 binding to the channel, indicating that Ca2+-independent CaM binding contributes to the facilitation mechanism.
Ca2 Binding (binding) of CaM
2) Confidence 0.03 Published 2010 Journal PLoS ONE Section Body Doc Link PMC2867956 Disease Relevance 0 Pain Relevance 0.09
CaM binding, secondary to rises in intracellular Ca2+, displaces the N-terminal domain which may then form a homologous interaction with an identical domain from a second subunit.
Ca2 Binding (binding) of CaM
3) Confidence 0.03 Published 2010 Journal PLoS ONE Section Abstract Doc Link PMC2867956 Disease Relevance 0 Pain Relevance 0.04

General Comments

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