INT116055

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Context Info
Confidence 0.80
First Reported 2004
Last Reported 2010
Negated 0
Speculated 0
Reported most in Body
Documents 33
Total Number 33
Disease Relevance 2.22
Pain Relevance 5.58

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

cytosol (PRKG1) signal transduction (PRKG1) plasma membrane (PRKG1)
cytoplasm (PRKG1)
Anatomy Link Frequency
tail 3
intermediary 3
platelet 2
synapse 2
smooth muscle 1
PRKG1 (Homo sapiens)
Pain Link Frequency Relevance Heat
Dorsal horn neuron 40 100.00 Very High Very High Very High
agonist 797 99.82 Very High Very High Very High
Kinase C 31 99.80 Very High Very High Very High
Serotonin 80 98.76 Very High Very High Very High
antagonist 28 98.64 Very High Very High Very High
Action potential 85 97.84 Very High Very High Very High
Neurotransmitter 94 97.56 Very High Very High Very High
nMDA receptor 208 97.52 Very High Very High Very High
central sensitization 37 95.08 Very High Very High Very High
qutenza 64 91.92 High High
Disease Link Frequency Relevance Heat
Apoptosis 35 99.28 Very High Very High Very High
Hypertension 43 98.12 Very High Very High Very High
Anxiety Disorder 153 91.36 High High
Injury 31 91.32 High High
Obsessive-compulsive Disorder 7 88.52 High High
Depression 80 86.44 High High
Nervous System Injury 11 85.36 High High
Death 6 83.24 Quite High
Nociception 33 76.76 Quite High
Familial Adenomatous Polyposis 7 68.32 Quite High

Sentences Mentioned In

Key: Protein Mutation Event Anatomy Negation Speculation Pain term Disease term
A major NO–PKG transduction pathway in smooth muscle and platelets is through the IP3 receptor-associated protein IRAG which, when phosphorylated by PKG1?
Phosphorylation (phosphorylated) of PKG in smooth muscle
1) Confidence 0.80 Published 2008 Journal The European Journal of Neuroscience Section Body Doc Link PMC2610389 Disease Relevance 0 Pain Relevance 0.11
Interestingly, our second candidate, PRKG1, a serine-threonine kinase, also activates opening of the KCNMA1 channel via phosphorylation [39], [40].
Phosphorylation (phosphorylation) of PRKG1
2) Confidence 0.75 Published 2010 Journal PLoS ONE Section Body Doc Link PMC2935366 Disease Relevance 0.16 Pain Relevance 0
Binding of cGMP led to the formation of a complex between PKGII and GluR1 and the phosphorylation of GluR1 on a serine residue (serine-845) that facilitates its delivery to extrasynaptic sites, priming insertion into the synapse.
Phosphorylation (phosphorylation) of PKG in synapse
3) Confidence 0.61 Published 2008 Journal The European Journal of Neuroscience Section Body Doc Link PMC2610389 Disease Relevance 0 Pain Relevance 0.22
Binding of cGMP led to the formation of a complex between PKGII and GluR1 and the phosphorylation of GluR1 on a serine residue (serine-845) that facilitates its delivery to extrasynaptic sites, priming insertion into the synapse.
Phosphorylation (phosphorylation) of PKG in synapse
4) Confidence 0.61 Published 2008 Journal The European Journal of Neuroscience Section Body Doc Link PMC2610389 Disease Relevance 0 Pain Relevance 0.22
was directly impaired by prostacyclin and NO through protein kinase (PK)A- and PKG-dependent phosphorylation, respectively, signaling by TP?
Phosphorylation (phosphorylation) of PKG
5) Confidence 0.39 Published 2008 Journal Cellular Signalling Section Abstract Doc Link PMC2681257 Disease Relevance 0 Pain Relevance 0
is not subject to direct PKA or PKG phosphorylation, its signaling by prostacyclin or NO may only be regulated at downstream intermediary level(s), such as at the level of RhoA phosphorylation.
Phosphorylation (phosphorylation) of PKG in intermediary
6) Confidence 0.39 Published 2008 Journal Cellular Signalling Section Body Doc Link PMC2681257 Disease Relevance 0 Pain Relevance 0
is not a direct target for either PKA or PKG phosphorylation or inhibition, but its RhoA-mediated signaling would be sensitive to RhoA phosphorylation by either second messenger kinase.
Phosphorylation (phosphorylation) of PKG
7) Confidence 0.39 Published 2008 Journal Cellular Signalling Section Body Doc Link PMC2681257 Disease Relevance 0 Pain Relevance 0
Specifically, prostacyclin-desensitization occurs by direct PKA phosphorylation of Ser329 while NO-desensitization occurs through PKG phosphorylation of Ser331, both within the unique C-tail domain of TP?
Phosphorylation (phosphorylation) of PKG in tail
8) Confidence 0.39 Published 2008 Journal Cellular Signalling Section Body Doc Link PMC2681257 Disease Relevance 0 Pain Relevance 0
itself, namely through site specific prostacyclin-induced PKA (at Ser329) and NO-induced PKG (at Ser331) phosphorylation rather than at some other intermediary in the RhoA signaling cascade.
Phosphorylation (phosphorylation) of PKG in intermediary
9) Confidence 0.38 Published 2008 Journal Cellular Signalling Section Body Doc Link PMC2681257 Disease Relevance 0 Pain Relevance 0.04
, is also desensitized by the platelet antagonist /vasodilator nitric oxide (NO), involving direct NO/cGMP-dependent PKG phosphorylation of TP?
Phosphorylation (phosphorylation) of PKG in platelet associated with antagonist
10) Confidence 0.38 Published 2008 Journal Cellular Signalling Section Body Doc Link PMC2681257 Disease Relevance 0 Pain Relevance 0.05
undergoes agonist-induced PKG phosphorylation, we investigated the effect of KT 5823 on TP?
Phosphorylation (phosphorylation) of PKG associated with agonist
11) Confidence 0.36 Published 2007 Journal Biochim Biophys Acta Section Body Doc Link PMC2680961 Disease Relevance 0 Pain Relevance 0.22
is not a target for NO-mediated heterologous desensitization or PKG phosphorylation [35], neither KT 5823, LY 83583 nor l-NAME had any measurable effect on TP? 
Phosphorylation (phosphorylation) of PKG
12) Confidence 0.36 Published 2007 Journal Biochim Biophys Acta Section Body Doc Link PMC2680961 Disease Relevance 0 Pain Relevance 0.20
is indeed a direct target of NO/PKG phosphorylation and heterologous desensitization [35].
Phosphorylation (phosphorylation) of PKG
13) Confidence 0.36 Published 2007 Journal Biochim Biophys Acta Section Body Doc Link PMC2680961 Disease Relevance 0 Pain Relevance 0.10
It is noteworthy that Ser329 has previously been identified as a target residue for PKA phosphorylation [33] while Ser331 was identified as a target for PKG phosphorylation [35] and Thr337 as a target for PKC phosphorylation [32].
Phosphorylation (phosphorylation) of PKG
14) Confidence 0.36 Published 2007 Journal Biochim Biophys Acta Section Body Doc Link PMC2680961 Disease Relevance 0 Pain Relevance 0.04
, is subject to desensitization in response to the potent vasodilator nitric oxide (NO) that occurs through direct type 1 PKG-mediated phosphorylation where Ser331 was identified as the PKG phospho-target [35].
Phosphorylation (phosphorylation) of PKG-mediated
15) Confidence 0.36 Published 2007 Journal Biochim Biophys Acta Section Body Doc Link PMC2680961 Disease Relevance 0 Pain Relevance 0.17
-regulated PKC activation and phosphorylation of Ser145 and Thr337 and another involving eNOS phosphorylation and activation leading the NO/cGMP-regulated PKG phosphorylation of Ser331.
Phosphorylation (phosphorylation) of PKG
16) Confidence 0.36 Published 2007 Journal Biochim Biophys Acta Section Body Doc Link PMC2680961 Disease Relevance 0 Pain Relevance 0.16
, is also a target for nitric oxide (NO)-induced heterologous desensitization of signalling that occurs through direct cGMP-dependent PKG/cGK phosphorylation at Ser331 also within its C-tail [35].
Phosphorylation (phosphorylation) of PKG in tail
17) Confidence 0.36 Published 2007 Journal Biochim Biophys Acta Section Body Doc Link PMC2680961 Disease Relevance 0 Pain Relevance 0.06
entails a closed feedback loop involving eNOS phosphorylation/activation, NO generation and subsequent PKG phosphorylation is a mechanism not typically associated with homologous desensitization of GPCRs in general, it is also in agreement with our previous studies demonstrating that TP?
Phosphorylation (phosphorylation) of PKG
18) Confidence 0.36 Published 2007 Journal Biochim Biophys Acta Section Body Doc Link PMC2680961 Disease Relevance 0 Pain Relevance 0.05
A major NO–PKG transduction pathway in smooth muscle and platelets is through the IP3 receptor-associated protein IRAG which, when phosphorylated by PKG1?
Phosphorylation (phosphorylated) of PKG in platelets
19) Confidence 0.27 Published 2008 Journal The European Journal of Neuroscience Section Body Doc Link PMC2610389 Disease Relevance 0 Pain Relevance 0.11
Activated PKG has been shown to phosphorylate ?
Phosphorylation (phosphorylate) of PKG
20) Confidence 0.23 Published 2006 Journal Invest New Drugs Section Body Doc Link PMC2780666 Disease Relevance 0.31 Pain Relevance 0.41

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