INT57442

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Context Info
Confidence 0.70
First Reported 1994
Last Reported 2011
Negated 0
Speculated 1
Reported most in Body
Documents 98
Total Number 99
Disease Relevance 31.58
Pain Relevance 41.04

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

mitochondrion (Prkca) endoplasmic reticulum (Prkca) enzyme binding (Prkca)
protein complex (Prkca) cytoplasm (Prkca) cytosol (Prkca)
Anatomy Link Frequency
neurons 10
neuronal 2
tail 1
brain 1
neurite 1
Prkca (Mus musculus)
Pain Link Frequency Relevance Heat
Kinase C 2679 100.00 Very High Very High Very High
agonist 234 99.84 Very High Very High Very High
Morphine 409 99.70 Very High Very High Very High
Pain 448 99.44 Very High Very High Very High
Dorsal horn 94 99.36 Very High Very High Very High
Dorsal horn neuron 66 99.14 Very High Very High Very High
qutenza 985 99.02 Very High Very High Very High
Central nervous system 264 98.96 Very High Very High Very High
long-term potentiation 201 98.88 Very High Very High Very High
Spinal cord 226 98.60 Very High Very High Very High
Disease Link Frequency Relevance Heat
Virus Diseases 1786 99.88 Very High Very High Very High
Targeted Disruption 379 99.40 Very High Very High Very High
Infection 449 99.36 Very High Very High Very High
Breast Cancer 5 99.32 Very High Very High Very High
Hypersensitivity 44 98.80 Very High Very High Very High
Pain 505 98.20 Very High Very High Very High
INFLAMMATION 755 97.70 Very High Very High Very High
Nociception 601 97.30 Very High Very High Very High
Stress 151 97.24 Very High Very High Very High
Neuroblastoma 16 97.04 Very High Very High Very High

Sentences Mentioned In

Key: Protein Mutation Event Anatomy Negation Speculation Pain term Disease term
PKC phosphorylation inhibits endocytosis (PKC hypothesis).
Phosphorylation (phosphorylation) of PKC associated with kinase c
1) Confidence 0.70 Published 2004 Journal Ann. N. Y. Acad. Sci. Section Abstract Doc Link 15542739 Disease Relevance 0.07 Pain Relevance 1.18
From current studies, it is known that various phosphorylation steps, such as protein kinase C (PKC) and G protein-coupled receptor (GPCR) kinase (GRK) regulate endocytosis.
Phosphorylation (phosphorylation) of PKC associated with kinase c
2) Confidence 0.69 Published 2004 Journal Ann. N. Y. Acad. Sci. Section Abstract Doc Link 15542739 Disease Relevance 0 Pain Relevance 0.91
The phosphorylation of MARCKS by PKC is implicated in actin-dependent cytoskeletal plasticity [41] and has been associated with PKC-mediated enhancement of neurotransmitter release, as well as with persistence of LTP in vivo [42].
Phosphorylation (phosphorylation) of PKC associated with neurotransmitter, kinase c and long-term potentiation
3) Confidence 0.65 Published 2006 Journal PLoS Pathogens Section Body Doc Link PMC1401496 Disease Relevance 0.79 Pain Relevance 0.72
Interestingly, inhibition of the phosphorylation of endogenous PKC substrates was also observed after transfection of neurons with BDV P.
Phosphorylation (phosphorylation) of PKC in neurons associated with virus diseases and kinase c
4) Confidence 0.65 Published 2006 Journal PLoS Pathogens Section Body Doc Link PMC1401496 Disease Relevance 0.61 Pain Relevance 0.69
In contrast, the phosphorylation of myristoylated alanine-rich C kinase substrate (MARCKS), a major PKC substrate in neurons [31], was severely impaired in BDV-infected neurons following treatment with glycine (Figure 4D).
Phosphorylation (phosphorylation) of PKC in neurons associated with virus diseases and kinase c
5) Confidence 0.65 Published 2006 Journal PLoS Pathogens Section Body Doc Link PMC1401496 Disease Relevance 0.84 Pain Relevance 0.20
Previously, it has been shown that the BDV P is phosphorylated by PKC in vivo and in vitro [38].
Phosphorylation (phosphorylated) of PKC associated with virus diseases and kinase c
6) Confidence 0.65 Published 2006 Journal PLoS Pathogens Section Body Doc Link PMC1401496 Disease Relevance 0.96 Pain Relevance 0.66
Rather, BDV blocked the phosphorylation of PKC neuronal substrates, such as MARCKS and Munc18, which play essential roles in vesicular cycling.
Phosphorylation (phosphorylation) of PKC in neuronal associated with virus diseases and kinase c
7) Confidence 0.65 Published 2006 Journal PLoS Pathogens Section Body Doc Link PMC1401496 Disease Relevance 0.78 Pain Relevance 0.68
It is conceivable that the activity of PKC depends on the accessibility and the concentration of its substrates in the cell, and we postulate that the accumulation of a viral protein that can serve as a substrate for PKC may compete with the phosphorylation of endogenous PKC targets.
Phosphorylation (phosphorylation) of PKC associated with kinase c
8) Confidence 0.65 Published 2006 Journal PLoS Pathogens Section Body Doc Link PMC1401496 Disease Relevance 0.58 Pain Relevance 0.56
Thus, we hypothesized that P could compete with the phosphorylation of endogenous PKC substrates.
Phosphorylation (phosphorylation) of PKC associated with kinase c
9) Confidence 0.65 Published 2006 Journal PLoS Pathogens Section Body Doc Link PMC1401496 Disease Relevance 0.91 Pain Relevance 0.56
P, a cofactor for the viral polymerase complex, is abundantly expressed in the CNS following infection and was previously shown to be phosphorylated by PKC [38], consistent with our findings that P is phosphorylated at serine residues following PMA treatment.
Phosphorylation (phosphorylated) of PKC associated with kinase c, central nervous system and infection
10) Confidence 0.65 Published 2006 Journal PLoS Pathogens Section Body Doc Link PMC1401496 Disease Relevance 0.61 Pain Relevance 0.66
Furthermore, PKC-dependent phosphorylation of the presynaptic protein Munc18 regulates neurotransmitter release and has been implicated in presynaptic plasticity [35].
Phosphorylation (phosphorylation) of PKC associated with neurotransmitter and kinase c
11) Confidence 0.65 Published 2006 Journal PLoS Pathogens Section Body Doc Link PMC1401496 Disease Relevance 0.76 Pain Relevance 0.68
BDV replication is tightly regulated by complex mechanisms and the phosphorylation of P by PKC could increase the activity of the viral polymerase complex, thereby contributing to BDV adaptation to persistence in neurons [45,46].
Phosphorylation (phosphorylation) of PKC in neurons associated with virus diseases and kinase c
12) Confidence 0.64 Published 2006 Journal PLoS Pathogens Section Body Doc Link PMC1401496 Disease Relevance 0.71 Pain Relevance 0.45
We propose that the stimulation of synaptic connections of infected neurons, for example during learning, leads to increased phosphorylation of P consecutive to PKC activation and hence to increased viral replication and spread in the CNS, at the expense of behavioral disabilities for the host.
Phosphorylation (phosphorylation) of PKC in neurons associated with kinase c and central nervous system
13) Confidence 0.64 Published 2006 Journal PLoS Pathogens Section Body Doc Link PMC1401496 Disease Relevance 0.63 Pain Relevance 0.39
Protein kinase C (PKC) is able to phosphorylate several cellular components that serve as key regulatory components in signal transduction pathways of nociceptor excitation and sensitisation.
Phosphorylation (phosphorylate) of PKC in nociceptor associated with kinase c and nociceptor
14) Confidence 0.54 Published 2005 Journal Pain Section Abstract Doc Link 16099101 Disease Relevance 0.22 Pain Relevance 0.23
PKC-dependent myristoylated alanine-rich C kinase substrate phosphorylation in epsilonPKC knock-out cells revealed that only a subset of the peptides were selective for epsilonPKC over other PKC isozymes.
Phosphorylation (phosphorylation) of PKC-dependent associated with targeted disruption and kinase c
15) Confidence 0.52 Published 2007 Journal J. Biol. Chem. Section Abstract Doc Link 17142835 Disease Relevance 0.43 Pain Relevance 0.52
Finally, we show that transfection of BDV phosphoprotein (P) in neurons leads to impaired PKC-dependent phosphorylation.
Phosphorylation (phosphorylation) of PKC in neurons associated with virus diseases and kinase c
16) Confidence 0.50 Published 2006 Journal PLoS Pathogens Section Body Doc Link PMC1401496 Disease Relevance 1.07 Pain Relevance 0.20
The authors also provide evidence that the viral phosphoprotein may be responsible for this interference, possibly by competing with the phosphorylation of endogenous cellular PKC substrates.
Phosphorylation (phosphorylation) of PKC associated with kinase c
17) Confidence 0.50 Published 2006 Journal PLoS Pathogens Section Abstract Doc Link PMC1401496 Disease Relevance 0.78 Pain Relevance 0.23
In particular, extracellular-regulated kinase (ERK) 1/2, protein kinase A (PKA), Ca2+/calmodulin-dependent kinase (CaMK) II, and PKC phosphorylate presynaptic proteins that modulate SV recycling [28,29].
Phosphorylation (phosphorylate) of PKC associated with kinase c
18) Confidence 0.50 Published 2006 Journal PLoS Pathogens Section Body Doc Link PMC1401496 Disease Relevance 0.61 Pain Relevance 0.20
We then analyzed the phosphorylation of PKC substrates following direct stimulation of PKC by PMA.
Phosphorylation (phosphorylation) of PKC associated with kinase c
19) Confidence 0.50 Published 2006 Journal PLoS Pathogens Section Body Doc Link PMC1401496 Disease Relevance 0.58 Pain Relevance 0.54
We also showed that P was phosphorylated at serine residues following treatment with PMA (Figure 8D), in agreement with the previous demonstration that P is phosphorylated by PKC.


Phosphorylation (phosphorylated) of PKC associated with kinase c
20) Confidence 0.50 Published 2006 Journal PLoS Pathogens Section Body Doc Link PMC1401496 Disease Relevance 0.59 Pain Relevance 0.24

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