INT170727

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Context Info
Confidence 0.01
First Reported 2001
Last Reported 2001
Negated 0
Speculated 0
Reported most in Body
Documents 1
Total Number 15
Disease Relevance 0.13
Pain Relevance 0.28

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

cytoplasm (Grm5, Calm2) nucleoplasm (Calm2) signal transducer activity (Grm5)
cytosol (Calm2) plasma membrane (Grm5) cytoskeleton (Calm2)
Anatomy Link Frequency
tail 1
Grm5 (Rattus norvegicus)
Calm2 (Rattus norvegicus)
Pain Link Frequency Relevance Heat
Glutamate 180 76.68 Quite High
Glutamate receptor 60 65.28 Quite High
Neuronal excitability 15 52.96 Quite High
imagery 30 5.00 Very Low Very Low Very Low
addiction 15 5.00 Very Low Very Low Very Low
tetrodotoxin 15 5.00 Very Low Very Low Very Low
Disease Link Frequency Relevance Heat
Ganglion Cysts 90 66.80 Quite High
Cancer 15 38.08 Quite Low
Apoptosis 15 37.04 Quite Low

Sentences Mentioned In

Key: Protein Mutation Event Anatomy Negation Speculation Pain term Disease term
The data imply two possible mechanisms for the effect of Siah1a on mGluR signaling: First, CaM association with group I mGluRs increases G protein coupling (or perhaps is required, as may be the case with group III mGluRs).
mGluRs Binding (association) of CaM
1) Confidence 0.01 Published 2001 Journal BMC Neurosci Section Body Doc Link PMC58838 Disease Relevance 0 Pain Relevance 0
Calmodulin (CaM), a calcium binding protein intricately involved in intracellular signaling, interacts with the C-terminal tail of group I mGluRs [25].
mGluRs Binding (interacts) of CaM in tail
2) Confidence 0.01 Published 2001 Journal BMC Neurosci Section Body Doc Link PMC58838 Disease Relevance 0 Pain Relevance 0.07
Finally, coexpression of CaM reversed the effect of Siah1a on mGluR5b, indicating that the interaction of CaM and Siah1a in binding to group I mGluRs plays a novel and important role in mGluR function.


mGluRs Binding (interaction) of CaM
3) Confidence 0.01 Published 2001 Journal BMC Neurosci Section Body Doc Link PMC58838 Disease Relevance 0.07 Pain Relevance 0.03
This model predicts that Siah1a association produces its effect by disrupting the interaction of CaM with the group I mGluRs.
mGluRs Binding (interaction) of CaM
4) Confidence 0.01 Published 2001 Journal BMC Neurosci Section Body Doc Link PMC58838 Disease Relevance 0 Pain Relevance 0
For example, group I and group III mGluRs are both known to bind Calmodulin (CaM) [25,26].
mGluRs Binding (bind) of CaM
5) Confidence 0.01 Published 2001 Journal BMC Neurosci Section Body Doc Link PMC58838 Disease Relevance 0 Pain Relevance 0.03
The data imply two possible mechanisms for the effect of Siah1a on mGluR signaling: First, CaM association with group I mGluRs increases G protein coupling (or perhaps is required, as may be the case with group III mGluRs).
mGluRs Binding (association) of CaM
6) Confidence 0.01 Published 2001 Journal BMC Neurosci Section Body Doc Link PMC58838 Disease Relevance 0 Pain Relevance 0
Finally, CaM binding to the mGluRs did not appear to be Ca2+-dependent.
mGluRs Binding (binding) of CaM
7) Confidence 0.01 Published 2001 Journal BMC Neurosci Section Body Doc Link PMC58838 Disease Relevance 0 Pain Relevance 0
Although CaM has been known to associate with group I mGluRs for some time, the functional role of this interaction is unknown.
mGluRs Binding (associate) of CaM
8) Confidence 0.01 Published 2001 Journal BMC Neurosci Section Body Doc Link PMC58838 Disease Relevance 0 Pain Relevance 0.03
CaM binding to both group I and group III mGluRs can be inhibited by serine/threonine phosphorylation at specific sites [25,28].
mGluRs Binding (binding) of CaM
9) Confidence 0.01 Published 2001 Journal BMC Neurosci Section Body Doc Link PMC58838 Disease Relevance 0 Pain Relevance 0
Finally, coexpression of CaM reversed the effect of Siah1a on mGluR5b, indicating that the interaction of CaM and Siah1a in binding to group I mGluRs plays a novel and important role in mGluR function.


mGluRs Binding (binding) of CaM
10) Confidence 0.01 Published 2001 Journal BMC Neurosci Section Body Doc Link PMC58838 Disease Relevance 0.07 Pain Relevance 0.03
By analogy to group III mGluRs, the ability of Siah1a to compete with CaM for binding to group I mGluRs was considered a potential mechanism for the actions of Siah1a on group I mGluR-mediated calcium current inhibition.
mGluRs Binding (binding) of CaM
11) Confidence 0.01 Published 2001 Journal BMC Neurosci Section Body Doc Link PMC58838 Disease Relevance 0 Pain Relevance 0
Phosphorylation of the receptors at specific sites prevents CaM binding to mGluRs [25].
mGluRs Binding (binding) of CaM
12) Confidence 0.01 Published 2001 Journal BMC Neurosci Section Body Doc Link PMC58838 Disease Relevance 0 Pain Relevance 0.06
However, CaM can also interact with group III mGluRs [26,28].
mGluRs Binding (interact) of CaM
13) Confidence 0.01 Published 2001 Journal BMC Neurosci Section Body Doc Link PMC58838 Disease Relevance 0 Pain Relevance 0.03
In this case, it must be assumed that under control conditions (cells heterologously expressing only the receptors), mGluRs associate with natively-expressed CaM.
mGluRs Binding (associate) of CaM
14) Confidence 0.01 Published 2001 Journal BMC Neurosci Section Body Doc Link PMC58838 Disease Relevance 0 Pain Relevance 0
Recent data suggests that the association of CaM with group III mGluRs is necessary for normal G protein activation [27].
mGluRs Binding (association) of CaM
15) Confidence 0.01 Published 2001 Journal BMC Neurosci Section Body Doc Link PMC58838 Disease Relevance 0 Pain Relevance 0

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