INT112905

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Context Info
Confidence 0.82
First Reported 2003
Last Reported 2010
Negated 0
Speculated 0
Reported most in Body
Documents 15
Total Number 16
Disease Relevance 2.78
Pain Relevance 2.30

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

embryo development (Cdk5) cytoplasm (Cdk5) cytosol (Cdk5)
nucleocytoplasmic transport (Cdk5) cell death (Cdk5) nucleolus (Cdk5)
Anatomy Link Frequency
growth cones 1
cingulate cortex 1
synapse 1
Cdk5 (Mus musculus)
Pain Link Frequency Relevance Heat
Morphine 7 99.40 Very High Very High Very High
Calcium channel 13 99.30 Very High Very High Very High
ischemia 24 98.64 Very High Very High Very High
Neurotransmitter 18 97.76 Very High Very High Very High
Dopamine 521 97.60 Very High Very High Very High
Opioid 4 94.72 High High
Neuronal excitability 18 94.08 High High
adenocard 7 93.88 High High
Glutamate 132 93.12 High High
Neuropeptide 3 88.60 High High
Disease Link Frequency Relevance Heat
Transient Ischemic Attack 1 99.40 Very High Very High Very High
Shock 54 98.52 Very High Very High Very High
Injury 10 95.84 Very High Very High Very High
Convulsion 68 89.68 High High
Cv Unclassified Under Development 14 84.64 Quite High
Targeted Disruption 125 80.16 Quite High
Disease 43 77.80 Quite High
Drug Dependence 2 75.00 Quite High
Alzheimer's Dementia 5 74.08 Quite High
Death 31 72.12 Quite High

Sentences Mentioned In

Key: Protein Mutation Event Anatomy Negation Speculation Pain term Disease term
The level of phosphorylated-cdk5 was significantly increased in the cingulate cortex of mice showing the morphine-induced rewarding effect.
Phosphorylation (phosphorylated) of cdk5 in cingulate cortex associated with morphine
1) Confidence 0.82 Published 2005 Journal J. Neurochem. Section Abstract Doc Link 15935062 Disease Relevance 0.14 Pain Relevance 0.52
Cdk5 has specifically been implicated in exocytosis and endocytosis via phosphorylation of numerous substrates including synapsin, amphiphysin I, dynamin, and others [44]–[47].
Phosphorylation (phosphorylation) of Cdk5
2) Confidence 0.80 Published 2009 Journal PLoS ONE Section Body Doc Link PMC2695674 Disease Relevance 0.63 Pain Relevance 0.24
It has been shown that (R)-roscovitine reduced hyperphosporylation of the Tau protein, a major CDK5 target, after transient cerebral ischemia in rat, mainly by inhibiting CDK5 [21].
Phosphorylation (hyperphosporylation) of CDK5 associated with transient ischemic attack and ischemia
3) Confidence 0.68 Published 2010 Journal PLoS ONE Section Body Doc Link PMC2920814 Disease Relevance 0.43 Pain Relevance 0.12
On the other hand, DARPP-32 becomes an inhibitor of PKA when it is phosphorylated on Thr75 by cyclin-dependent kinase 5 (Cdk5).
Phosphorylation (phosphorylated) of Cdk5
4) Confidence 0.55 Published 2010 Journal Frontiers in Neuroanatomy Section Body Doc Link PMC2955397 Disease Relevance 0.14 Pain Relevance 0.12
On the other hand, DARPP-32 becomes an inhibitor of PKA when it is phosphorylated on Thr75 by cyclin-dependent kinase 5 (Cdk5).
Phosphorylation (phosphorylated) of cyclin-dependent kinase 5
5) Confidence 0.55 Published 2010 Journal Frontiers in Neuroanatomy Section Body Doc Link PMC2955397 Disease Relevance 0.14 Pain Relevance 0.09
We have recently observed P2X3 receptor serine phosphorylation by Cdk5 to be a powerful negative regulator of receptor function [26].
Phosphorylation (phosphorylation) of Cdk5
6) Confidence 0.43 Published 2010 Journal Mol Pain Section Body Doc Link PMC2940876 Disease Relevance 0 Pain Relevance 0
Sema3A induced the phosphorylation and activation of Cdk5 by Fyn, which was essential for the collapse of sensory growth cones by Sema3A.
Phosphorylation (phosphorylation) of Cdk5 in growth cones associated with shock
7) Confidence 0.42 Published 2007 Journal BMC Dev Biol Section Body Doc Link PMC2217550 Disease Relevance 0.28 Pain Relevance 0.03
Fyn was also shown to phosphorylate Cdk5 and the PlexinA2 cytoplasmic domain [44].
Phosphorylation (phosphorylate) of Cdk5
8) Confidence 0.42 Published 2007 Journal BMC Dev Biol Section Body Doc Link PMC2217550 Disease Relevance 0.28 Pain Relevance 0.03
DARPP-32 is also phosphorylated by cyclin-dependent kinase 5 on Thr75, and the phosphorylated form of DARPP-32 at Thr75 inhibits protein kinase (PKA) activity.
Phosphorylation (phosphorylated) of cyclin-dependent kinase 5
9) Confidence 0.40 Published 2003 Journal Eur. J. Neurosci. Section Abstract Doc Link 12956723 Disease Relevance 0 Pain Relevance 0.21
Thr34 is phosphorylated by PKA and dephosphorylated by protein phosphatase 2B (PP2B or calcineurin) [16,21] whereas Thr75 is phosphorylated by the cyclin-dependent kinase 5 (cdk5) and dephosphorylated mainly by PP2A [15,17].
Phosphorylation (phosphorylated) of cdk5
10) Confidence 0.36 Published 2006 Journal PLoS Computational Biology Section Body Doc Link PMC1562452 Disease Relevance 0 Pain Relevance 0.35
Thr34 is phosphorylated by PKA and dephosphorylated by protein phosphatase 2B (PP2B or calcineurin) [16,21] whereas Thr75 is phosphorylated by the cyclin-dependent kinase 5 (cdk5) and dephosphorylated mainly by PP2A [15,17].
Phosphorylation (phosphorylated) of cyclin-dependent kinase 5
11) Confidence 0.36 Published 2006 Journal PLoS Computational Biology Section Body Doc Link PMC1562452 Disease Relevance 0 Pain Relevance 0.35
The catalytic subunit of PKA catalyses phosphorylation of DARPP-32 at Thr34 [73,107]; Cdk5 catalyses phosphorylation of DARPP-32 at Thr75 [15].
Phosphorylation (phosphorylation) of Cdk5
12) Confidence 0.35 Published 2006 Journal PLoS Computational Biology Section Body Doc Link PMC1562452 Disease Relevance 0 Pain Relevance 0.03
Little is known about the regulation of Cdk5, but experiments show that there is a basal level of phosphorylation at Thr75 due to Cdk5 activity [108].
Phosphorylation (phosphorylation) of Cdk5
13) Confidence 0.35 Published 2006 Journal PLoS Computational Biology Section Body Doc Link PMC1562452 Disease Relevance 0 Pain Relevance 0
This increases the stability of the p25-CDK5 complex, alters its subcellular localization, and eventually results in the hyperphosphorylation of tau [97].
Phosphorylation (hyperphosphorylation) of CDK5
14) Confidence 0.25 Published 2009 Journal Microb Cell Fact Section Body Doc Link PMC2674406 Disease Relevance 0.61 Pain Relevance 0
Because CASK is involved in synaptic targeting of N-type calcium channels (Maximov and Bezprozvanny, 2002), phosphorylation of CASK by CDK5 modulates presynaptic calcium influx and controls synapse formation (Samuels et al., 2007).
Phosphorylation (phosphorylation) of CDK5 in synapse associated with calcium channel
15) Confidence 0.23 Published 2008 Journal The Journal of Cell Biology Section Body Doc Link PMC2447900 Disease Relevance 0.08 Pain Relevance 0.12
In addition to spinogenesis, CASK also acts presynaptically to regulate synaptogenesis through a different mechanism: CDK5 phosphorylates residues S51 and S395 of CASK proteins, which enhances the interaction between CASK and N-type calcium channels but impairs the interaction between CASK and liprin-?
Phosphorylation (phosphorylates) of CDK5 associated with calcium channel
16) Confidence 0.23 Published 2008 Journal The Journal of Cell Biology Section Body Doc Link PMC2447900 Disease Relevance 0.05 Pain Relevance 0.09

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