INT12763

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Context Info
Confidence 0.82
First Reported 1991
Last Reported 2010
Negated 3
Speculated 0
Reported most in Abstract
Documents 167
Total Number 167
Disease Relevance 38.91
Pain Relevance 89.63

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

cytosol (Prkcg) plasma membrane (Prkcg) nucleus (Prkcg)
intracellular (Prkcg) response to stress (Prkcg) cytoplasm (Prkcg)
Anatomy Link Frequency
neurons 6
spinal cord 5
nucleus 3
spinal 3
DRGs 3
Prkcg (Rattus norvegicus)
Pain Link Frequency Relevance Heat
Kinase C 3314 100.00 Very High Very High Very High
qutenza 905 100.00 Very High Very High Very High
agonist 459 100.00 Very High Very High Very High
Spinal cord 408 100.00 Very High Very High Very High
nMDA receptor 380 100.00 Very High Very High Very High
opioid receptor 353 100.00 Very High Very High Very High
Morphine 201 100.00 Very High Very High Very High
Dorsal horn neuron 94 100.00 Very High Very High Very High
Dorsal horn 92 100.00 Very High Very High Very High
nociceptor 84 100.00 Very High Very High Very High
Disease Link Frequency Relevance Heat
Stress 105 100.00 Very High Very High Very High
Diabetes Mellitus 368 99.88 Very High Very High Very High
Pain 553 99.62 Very High Very High Very High
INFLAMMATION 313 99.48 Very High Very High Very High
Nervous System Injury 96 99.44 Very High Very High Very High
Ganglion Cysts 636 99.40 Very High Very High Very High
Hyperalgesia 307 99.34 Very High Very High Very High
Nociception 506 99.22 Very High Very High Very High
Cv General 4 Under Development 87 99.18 Very High Very High Very High
Diabetic Neuropathy 74 99.12 Very High Very High Very High

Sentences Mentioned In

Key: Protein Mutation Event Anatomy Negation Speculation Pain term Disease term
Thus, tolerance produced by morphine infusion is dependent upon an increase in local phosphorylating activity by PKC.
Phosphorylation (phosphorylating) of PKC associated with kinase c, tolerance and morphine
1) Confidence 0.82 Published 2000 Journal Pain Section Abstract Doc Link 10781912 Disease Relevance 0 Pain Relevance 1.75
I.t. morphine infusion, but not saline, produced a 2-fold increase in dorsal horn PKC phosphorylating activity and in the expression of PKCalpha/gamma.
Phosphorylation (phosphorylating) of PKC in dorsal horn associated with kinase c, dorsal horn and morphine
2) Confidence 0.82 Published 2000 Journal Pain Section Abstract Doc Link 10781912 Disease Relevance 0 Pain Relevance 1.85
Phosphorylation, in particular by protein kinase C (PKC), modulates spinal sensory transmission and nociceptive behaviors.
Phosphorylation (Phosphorylation) of PKC in spinal associated with nociception and kinase c
3) Confidence 0.81 Published 2004 Journal J Pain Section Abstract Doc Link 15336637 Disease Relevance 0.10 Pain Relevance 0.31
These results indicate that activation of MOR coupled to G-proteins inhibits VDCC, and that this G-protein-mediated inhibition is antagonized by PKC-dependent phosphorylation.
Phosphorylation (phosphorylation) of PKC associated with opioid receptor
4) Confidence 0.80 Published 2004 Journal Brain Res. Section Abstract Doc Link 15261106 Disease Relevance 0.07 Pain Relevance 0.51
These results suggest that painful diabetic neuropathy is associated with altered cell-specific expression of the VR1 receptor that is coupled to increased function through PKC-mediated phosphorylation, oligomerization, and targeted expression on the cell surface membrane.
Phosphorylation (phosphorylation) of PKC associated with painful diabetic neuropathy and kinase c
5) Confidence 0.80 Published 2005 Journal J. Biol. Chem. Section Abstract Doc Link 15513920 Disease Relevance 0.93 Pain Relevance 0.81
Protein kinase C (PKC)-delta, PKC-gamma, stress-activated protein kinase, cAMP-dependent protein kinase beta isoform, Janus protein kinase, and phosphofructokinase M were all down regulated chronically with citalopram and fluoxetine, but not with acute fluoxetine.
Neg (not) Phosphorylation (regulated) of PKC associated with stress, kinase c and fluoxetine
6) Confidence 0.79 Published 2002 Journal Neurosci. Lett. Section Abstract Doc Link 12435479 Disease Relevance 0.10 Pain Relevance 0.66
The use of protein kinase C (PKC) inhibitors and activator, as well as the systematic mutation of potential PKC phosphorylation sites in NAC1, demonstrated that phosphorylation of residue S245 by PKC is a necessary event inducing diffuse NAC1 expression outside of the nucleus.
Phosphorylation (phosphorylation) of PKC in nucleus associated with kinase c
7) Confidence 0.79 Published 2005 Journal Eur. J. Neurosci. Section Abstract Doc Link 16045493 Disease Relevance 0 Pain Relevance 0.38
The use of protein kinase C (PKC) inhibitors and activator, as well as the systematic mutation of potential PKC phosphorylation sites in NAC1, demonstrated that phosphorylation of residue S245 by PKC is a necessary event inducing diffuse NAC1 expression outside of the nucleus.
Phosphorylation (phosphorylation) of PKC in nucleus associated with kinase c
8) Confidence 0.79 Published 2005 Journal Eur. J. Neurosci. Section Abstract Doc Link 16045493 Disease Relevance 0 Pain Relevance 0.40
The AMPA receptor subunits are also phosphorylated by PKC [27,29].
Phosphorylation (phosphorylated) of PKC associated with kinase c
9) Confidence 0.79 Published 2006 Journal Mol Pain Section Body Doc Link PMC1482680 Disease Relevance 0.15 Pain Relevance 0.92
Second, PKC could phosphorylate the NMDA or AMPA/kainite receptor to result in increase channel conductance or potentiation of glutamate gated currents that would be manifested as an increased excitability of the neuron [27-30].
Phosphorylation (phosphorylate) of PKC in neuron associated with glutamate and kinase c
10) Confidence 0.79 Published 2006 Journal Mol Pain Section Body Doc Link PMC1482680 Disease Relevance 0.05 Pain Relevance 1.37
Thus, SP, which is released in the spinal cord subsequent to persistent stimulation of small sensory afferents after tissue injury, may contribute to spinal hyperexcitability and persistent pain by enhancement of PKC-mediated phosphorylation of target molecules such as NMDA receptors.
Phosphorylation (phosphorylation) of PKC in spinal associated with pain, kinase c, nmda receptor, lasting pain, injury, hyperexcitability, spinal cord and substance p
11) Confidence 0.78 Published 2000 Journal Brain Res. Section Abstract Doc Link 10986346 Disease Relevance 0.49 Pain Relevance 1.27
Phosphorylation of NR1 by PKC increases surface expression of NMDA receptors, increases delivery of NMDA receptors to the surface and to the synapse [28,37,38].
Phosphorylation (Phosphorylation) of PKC in synapse associated with kinase c and nmda receptor
12) Confidence 0.78 Published 2006 Journal Mol Pain Section Body Doc Link PMC1482680 Disease Relevance 0.15 Pain Relevance 0.95
Both basal and PKC-mediated labeling of Goalpha with 32Pi was significantly less in DRGs from diabetic rats, supporting increased endogenous PKC-dependent phosphorylation of Goalpha.
Phosphorylation (phosphorylation) of PKC in DRGs associated with kinase c and diabetes mellitus
13) Confidence 0.75 Published 2003 Journal J. Neurochem. Section Abstract Doc Link 12887697 Disease Relevance 0.80 Pain Relevance 0.63
We examined the hypothesis that decreased inhibitory G protein function in diabetic neuropathy is associated with increased protein kinase C (PKC)-dependent phosphorylation of the Goalpha subunit.
Phosphorylation (phosphorylation) of PKC associated with kinase c and diabetic neuropathy
14) Confidence 0.75 Published 2003 Journal J. Neurochem. Section Abstract Doc Link 12887697 Disease Relevance 0.49 Pain Relevance 0.40
Phosphorylation of PKC-alpha was increased, PKC-betaII was unchanged and PKC-delta decreased in diabetic DRGs.
Phosphorylation (Phosphorylation) of PKC in DRGs associated with kinase c and diabetes mellitus
15) Confidence 0.75 Published 2003 Journal J. Neurochem. Section Abstract Doc Link 12887697 Disease Relevance 0.77 Pain Relevance 0.62
We have found that phosphorylation of a G-protein-coupled receptor by protein kinase C (PKC) disrupts modulation of ion channels by the receptor.
Phosphorylation (phosphorylation) of PKC associated with kinase c
16) Confidence 0.73 Published 1998 Journal J. Neurosci. Section Abstract Doc Link 9526000 Disease Relevance 0.08 Pain Relevance 0.62
The possibility that PKC acted by phosphorylating CB1 receptors was confirmed by demonstrating that PKC phosphorylated a single serine (S317) of a fusion protein incorporating the third intracellular loop of CB1.
Phosphorylation (phosphorylating) of PKC associated with kinase c and cannabinoid receptor
17) Confidence 0.72 Published 1998 Journal J. Neurosci. Section Abstract Doc Link 9526000 Disease Relevance 0.09 Pain Relevance 0.83
The possibility that PKC acted by phosphorylating CB1 receptors was confirmed by demonstrating that PKC phosphorylated a single serine (S317) of a fusion protein incorporating the third intracellular loop of CB1.
Phosphorylation (phosphorylated) of PKC associated with kinase c and cannabinoid receptor
18) Confidence 0.72 Published 1998 Journal J. Neurosci. Section Abstract Doc Link 9526000 Disease Relevance 0.08 Pain Relevance 0.82
Concurrently, oxaliplatin chronic treatment induced a specific upregulation of gamma isoforms of PKC and increased phosphorylation of gamma/epsilon PKC isoforms within thalamus and PAG.
Phosphorylation (phosphorylation) of PKC in thalamus associated with urological neuroanatomy and thalamus
19) Confidence 0.65 Published 2009 Journal Pain Section Abstract Doc Link 19683395 Disease Relevance 0.85 Pain Relevance 0.57
The mechanism of TMP action may be the allosteric regulation via acting on the large extracellular region of ATP receptor-ion channel complex (P2X receptors) and promoting the phosphorylation of PKC site of the N-terminus of P2X receptors.
Phosphorylation (phosphorylation) of PKC
20) Confidence 0.64 Published 2005 Journal Brain Res. Section Abstract Doc Link 15804430 Disease Relevance 0.07 Pain Relevance 0.04

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