INT97018

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Context Info
Confidence 0.43
First Reported 2001
Last Reported 2010
Negated 0
Speculated 0
Reported most in Body
Documents 7
Total Number 38
Disease Relevance 0.13
Pain Relevance 5.82

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

nucleoplasm (CALM3) small molecule metabolic process (CALM3) carbohydrate metabolic process (CALM3)
cytoplasm (CALM3) cytosol (CALM3) signal transduction (CALM3)
Anatomy Link Frequency
lobe 3
pore 1
CALM3 (Homo sapiens)
Pain Link Frequency Relevance Heat
TRP channel 128 99.84 Very High Very High Very High
mu opioid receptor 56 99.60 Very High Very High Very High
Morphine 12 98.40 Very High Very High Very High
adenocard 32 95.52 Very High Very High Very High
addiction 68 95.32 Very High Very High Very High
tolerance 6 94.72 High High
Opioid 4 94.32 High High
Analgesic 4 93.12 High High
agonist 100 93.04 High High
Calcium channel 34 88.00 High High
Disease Link Frequency Relevance Heat
Death 2 79.12 Quite High
Infection 4 51.96 Quite High
INFLAMMATION 26 12.24 Low Low
Apoptosis 4 5.00 Very Low Very Low Very Low
Shock 4 5.00 Very Low Very Low Very Low
Pain 2 5.00 Very Low Very Low Very Low
Fungal Infection 2 5.00 Very Low Very Low Very Low
Disease 2 5.00 Very Low Very Low Very Low
Stress 2 5.00 Very Low Very Low Very Low

Sentences Mentioned In

Key: Protein Mutation Event Anatomy Negation Speculation Pain term Disease term
CaM binding was deficient for variants R265H- and S268P-MOR, suggesting that domains for G protein coupling and CaM binding overlap partially.
CaM Binding (binding) of associated with mu opioid receptor
1) Confidence 0.43 Published 2001 Journal J. Biol. Chem. Section Abstract Doc Link 11457836 Disease Relevance 0 Pain Relevance 1.08
In conclusion, each of the three single nucleotide polymorphisms mapping to the i3 loop of MOR caused substantial changes in basal G protein coupling, CaM binding, or both.
CaM Binding (binding) of associated with mu opioid receptor
2) Confidence 0.43 Published 2001 Journal J. Biol. Chem. Section Abstract Doc Link 11457836 Disease Relevance 0 Pain Relevance 0.88
Moreover, domains within the i3 loop of MOR have been shown to interact with both G proteins and calmodulin (CaM).
CaM Binding (interact) of associated with mu opioid receptor
3) Confidence 0.33 Published 2001 Journal J. Biol. Chem. Section Abstract Doc Link 11457836 Disease Relevance 0 Pain Relevance 1.05
CaM binding was deficient for variants R265H- and S268P-MOR, suggesting that domains for G protein coupling and CaM binding overlap partially.
CaM Binding (binding) of associated with mu opioid receptor
4) Confidence 0.32 Published 2001 Journal J. Biol. Chem. Section Abstract Doc Link 11457836 Disease Relevance 0 Pain Relevance 1.03
For TRPM2, co-immunoprecipitation experiments demonstrated CaM1234 binding to the channel, indicating that Ca2+-independent CaM binding contributes to the facilitation mechanism.
CaM1234 Binding (binding) of
5) Confidence 0.15 Published 2010 Journal PLoS ONE Section Body Doc Link PMC2867956 Disease Relevance 0 Pain Relevance 0.09
All data provide strong evidence for an interaction in TRPV4 between an N-terminal domain represented by the P2 peptide and a site in the C terminus, P5, that also binds to CaM.
CaM Binding (binds) of
6) Confidence 0.15 Published 2010 Journal PLoS ONE Section Body Doc Link PMC2867956 Disease Relevance 0 Pain Relevance 0
How does CaM binding facilitate Ca2+ entry through TRPV4 at the molecular level?
CaM Binding (binding) of
7) Confidence 0.15 Published 2010 Journal PLoS ONE Section Body Doc Link PMC2867956 Disease Relevance 0 Pain Relevance 0.08
Thus, in contrast to some other TRP channels, where CaM binding is present at nanomolar Ca2+ concentrations [4], [29], CaM binding to TRPV4 depends on Ca2+ concentrations above those in resting cells.
CaM Binding (binding) of associated with trp channel
8) Confidence 0.15 Published 2010 Journal PLoS ONE Section Body Doc Link PMC2867956 Disease Relevance 0 Pain Relevance 0.08
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.
CaM Binding (binding) of
9) Confidence 0.15 Published 2010 Journal PLoS ONE Section Body Doc Link PMC2867956 Disease Relevance 0 Pain Relevance 0.07
Although CaM binding is a prerequisite for potentiation, the molecular mechanism that couples CaM binding to enhanced channel activity has not been resolved.
CaM Binding (binding) of
10) Confidence 0.15 Published 2010 Journal PLoS ONE Section Body Doc Link PMC2867956 Disease Relevance 0 Pain Relevance 0.14
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+.
CaM Binding (interaction) of
11) Confidence 0.15 Published 2010 Journal PLoS ONE Section Body Doc Link PMC2867956 Disease Relevance 0 Pain Relevance 0.08
Although CaM binding is a prerequisite for potentiation, the molecular mechanism that couples CaM binding to enhanced channel activity has not been resolved.
CaM Binding (binding) of
12) Confidence 0.15 Published 2010 Journal PLoS ONE Section Body Doc Link PMC2867956 Disease Relevance 0 Pain Relevance 0.13
This is in good agreement with a previous study [11] that demonstrated that TRPV4 mutants in which CaM binding to the C terminus is abolished result in channels not potentiated by Ca2+ addition.
CaM Binding (binding) of
13) Confidence 0.15 Published 2010 Journal PLoS ONE Section Body Doc Link PMC2867956 Disease Relevance 0 Pain Relevance 0
The Ca2+ concentration at which CaM binding to P5 was half-maximal is higher than the IC50 for steady-state inhibition of TRPV4 by intracellular Ca2+ in electrophysiological experiments (around 600 nM, [25]).
CaM Binding (binding) of
14) Confidence 0.15 Published 2010 Journal PLoS ONE Section Body Doc Link PMC2867956 Disease Relevance 0 Pain Relevance 0.09
Here, an N-terminal domain is capable of interacting with both the cyclic nucleotide binding region in the C terminus of the protein and Ca2+/CaM.
CaM Binding (interacting) of
15) Confidence 0.15 Published 2010 Journal PLoS ONE Section Body Doc Link PMC2867956 Disease Relevance 0 Pain Relevance 0
Taken together, the data indicate a higher affinity of the N-terminal binding site towards C2 than to a second N-terminal fragment, suggesting that in the resting state of the channel when CaM is not bound to the C-terminal binding site, the interaction between the N and C termini prevails.
CaM Binding (bound) of
16) Confidence 0.15 Published 2010 Journal PLoS ONE Section Body Doc Link PMC2867956 Disease Relevance 0 Pain Relevance 0
A second, homologous interaction between the N termini of adjacent TRPV4 subunits that is present when CaM is bound to the C-terminal site may contribute to conformational changes that lead to current facilitation (Fig. 8B), but we currently have no functional evidence in support of this.
CaM Binding (bound) of
17) Confidence 0.15 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.
CaM Binding (binding) of
18) Confidence 0.15 Published 2010 Journal PLoS ONE Section Body Doc Link PMC2867956 Disease Relevance 0 Pain Relevance 0.09
A possible explanation for the apparent discrepancy in the Ca2+ dependencies is that CaM binding to the full-length channel may occur at lower concentrations than to the short fragment used here.
CaM Binding (binding) of
19) Confidence 0.15 Published 2010 Journal PLoS ONE Section Body Doc Link PMC2867956 Disease Relevance 0 Pain Relevance 0.08
Fluorescence polarization experiments with the carboxyfluorescein-labeled CaM binding peptide, P5, as the tracer molecule (Fig. 1A, Table S1), showed that CaM binding was Ca2+-dependent and half-maximal at 3.2 µM Ca2+ (Fig. 1C).
CaM Binding (binding) of
20) Confidence 0.15 Published 2010 Journal PLoS ONE Section Body Doc Link PMC2867956 Disease Relevance 0 Pain Relevance 0.08

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