INT98457

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Context Info
Confidence 0.33
First Reported 2001
Last Reported 2009
Negated 0
Speculated 0
Reported most in Body
Documents 11
Total Number 11
Disease Relevance 0.12
Pain Relevance 2.57

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

mitochondrion (Ppp1cc) carbohydrate metabolic process (Ppp1cc) protein complex (Ppp1cc)
cytoplasm (Ppp1cc) chromosome (Ppp1cc) nucleolus (Ppp1cc)
Anatomy Link Frequency
chromaffin cell 1
Ppp1cc (Mus musculus)
Pain Link Frequency Relevance Heat
Glutamate 202 98.52 Very High Very High Very High
long-term potentiation 52 97.56 Very High Very High Very High
Dopamine 721 96.76 Very High Very High Very High
Kinase C 34 95.08 Very High Very High Very High
agonist 16 94.94 High High
Morphine 4 94.70 High High
Neurotransmitter 36 84.56 Quite High
nMDA receptor 20 83.16 Quite High
Potency 1 81.92 Quite High
adenocard 6 80.72 Quite High
Disease Link Frequency Relevance Heat
Bordatella Infection 2 59.80 Quite High
Depression 25 16.88 Low Low
Targeted Disruption 14 5.00 Very Low Very Low Very Low
Anxiety Disorder 8 5.00 Very Low Very Low Very Low
Adhesions 4 5.00 Very Low Very Low Very Low
Generalized Anxiety Disorder 4 5.00 Very Low Very Low Very Low
Stress 4 5.00 Very Low Very Low Very Low
Epilepsy 4 5.00 Very Low Very Low Very Low
Respiratory Failure 2 5.00 Very Low Very Low Very Low
Necrosis 2 5.00 Very Low Very Low Very Low

Sentences Mentioned In

Key: Protein Mutation Event Anatomy Negation Speculation Pain term Disease term
This may explain observations that activation of D2 receptors decreases phosphoThr34 and decreases the phosphorylation of PP1 substrates [21,64].
Phosphorylation (phosphorylation) of PP1
1) Confidence 0.33 Published 2006 Journal PLoS Computational Biology Section Body Doc Link PMC1562452 Disease Relevance 0 Pain Relevance 0.14
When phosphorylated at Thr34, DARPP-32 is a potent inhibitor of PP1 [14], whereas when phosphorylated at Thr75 DARPP-32 inhibits protein kinase A (PKA) [15].
Phosphorylation (phosphorylated) of PP1
2) Confidence 0.33 Published 2006 Journal PLoS Computational Biology Section Body Doc Link PMC1562452 Disease Relevance 0 Pain Relevance 0.39
Thus the model uses the same dephosphorylation rates for PP1 bound and unbound phosphoThr34 to reproduce experimental measurements.
Phosphorylation (dephosphorylation) of PP1
3) Confidence 0.33 Published 2006 Journal PLoS Computational Biology Section Body Doc Link PMC1562452 Disease Relevance 0 Pain Relevance 0
Phosphorylation of Ser 845 on the GluR1 subunit by cAMP-dependent kinase (PKA) increases insertion of AMPA receptors into the membrane, whereas dephosphorylation by protein phosphatase 1 (PP1) has the opposite effect [11,12].
Phosphorylation (dephosphorylation) of PP1
4) Confidence 0.25 Published 2006 Journal PLoS Computational Biology Section Body Doc Link PMC1562452 Disease Relevance 0 Pain Relevance 0.42
Since the ratio PKAc:PP1 controls AMPA channel phosphorylation, this larger increase in PKAc:PP1 would translate into more LTP due to paired stimulation.
Phosphorylation (phosphorylation) of PP1 associated with long-term potentiation
5) Confidence 0.25 Published 2006 Journal PLoS Computational Biology Section Body Doc Link PMC1562452 Disease Relevance 0 Pain Relevance 0.14
Thus, model simulations suggest that PKA activation, phosphorylation of DARPP-32 at Thr34, and subsequent PP1 inhibition, produced by conjunctive glutamate and D1 receptor stimulation, can produce LTP by increased phosphorylation of AMPA receptors.
Phosphorylation (phosphorylation) of PP1 associated with glutamate and long-term potentiation
6) Confidence 0.25 Published 2006 Journal PLoS Computational Biology Section Body Doc Link PMC1562452 Disease Relevance 0 Pain Relevance 0.74
Up-regulation of KEPI expression by morphine, an agonist at PKC-regulating G-protein-coupled mu receptors, provides a novel signaling paradigm in which the half-lives of serine/threonine phosphorylation events can be influenced by activities at G(i)/G(o)-coupled receptors that modulate KEPI expression, KEPI phosphorylation, and KEPI regulation of PP1 activity.
Phosphorylation (phosphorylation) of PP1 associated with kinase c, agonist and morphine
7) Confidence 0.22 Published 2002 Journal J. Biol. Chem. Section Abstract Doc Link 11812771 Disease Relevance 0 Pain Relevance 0.57
Calcineurin-mediated DARPP-32 dephosphorylation and PP-1 activation is a feedforward inhibitory pathway to CaMKII activation.
Phosphorylation (dephosphorylation) of PP-1
8) Confidence 0.20 Published 2009 Journal Mol Syst Biol Section Body Doc Link PMC2710870 Disease Relevance 0 Pain Relevance 0
The increase of Ca2+/Calmodulin additionally activates calcineurin that shifts the equilibrium towards the unphosphorylated form of DARPP-32, which has no effect on PP-1.
Phosphorylation (unphosphorylated) of PP-1
9) Confidence 0.18 Published 2008 Journal Frontiers in Molecular Neuroscience Section Body Doc Link PMC2526003 Disease Relevance 0 Pain Relevance 0
PP-1 can also directly dephosphorylate the GABAA receptor.
Phosphorylation (dephosphorylate) of PP-1
10) Confidence 0.18 Published 2008 Journal Frontiers in Molecular Neuroscience Section Body Doc Link PMC2526003 Disease Relevance 0 Pain Relevance 0.10
The alpha(1A) subunit of P/Q-type Ca(2+) channels was immunoprecipitated from chromaffin cell extracts and found to be phosphorylated in a PP1-sensitive manner by endogenous kinases in the immunoprecipitate.
Phosphorylation (phosphorylated) of PP1 in chromaffin cell
11) Confidence 0.07 Published 2001 Journal J. Biol. Chem. Section Abstract Doc Link 11583988 Disease Relevance 0.12 Pain Relevance 0.07

General Comments

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