INT196836

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Context Info
Confidence 0.00
First Reported 2006
Last Reported 2006
Negated 0
Speculated 0
Reported most in Body
Documents 1
Total Number 4
Disease Relevance 0
Pain Relevance 0

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

phosphatase activity (Phospho1) mitochondrion (Ppp1cc) carbohydrate metabolic process (Ppp1cc)
protein complex (Ppp1cc) cytoplasm (Ppp1cc) chromosome (Ppp1cc)
Ppp1cc (Mus musculus)
Phospho1 (Mus musculus)
Pain Link Frequency Relevance Heat
Dopamine 476 50.00 Quite Low
Glutamate 124 44.28 Quite Low
long-term potentiation 32 5.00 Very Low Very Low Very Low
projection neuron 16 5.00 Very Low Very Low Very Low
Action potential 16 5.00 Very Low Very Low Very Low
Neurotransmitter 12 5.00 Very Low Very Low Very Low
imagery 12 5.00 Very Low Very Low Very Low
nMDA receptor 8 5.00 Very Low Very Low Very Low
Calcium channel 8 5.00 Very Low Very Low Very Low
dopamine receptor 8 5.00 Very Low Very Low Very Low

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Sentences Mentioned In

Key: Protein Mutation Event Anatomy Negation Speculation Pain term Disease term
Nonetheless, the very high affinity of phosphoThr34 for PP1 implies that almost all phosphoThr34 is bound to PP1, and if Thr34 can be dephosphorylated only when unbound, phosphoThr34 increases to the amount of PP1.
PP1 Binding (affinity) of phosphoThr34
1) Confidence 0.00 Published 2006 Journal PLoS Computational Biology Section Body Doc Link PMC1562452 Disease Relevance 0 Pain Relevance 0
Nonetheless, the very high affinity of phosphoThr34 for PP1 implies that almost all phosphoThr34 is bound to PP1, and if Thr34 can be dephosphorylated only when unbound, phosphoThr34 increases to the amount of PP1.
PP1 Binding (bound) of phosphoThr34
2) Confidence 0.00 Published 2006 Journal PLoS Computational Biology Section Body Doc Link PMC1562452 Disease Relevance 0 Pain Relevance 0
Nonetheless, the very high affinity of phosphoThr34 for PP1 implies that almost all phosphoThr34 is bound to PP1, and if Thr34 can be dephosphorylated only when unbound, phosphoThr34 increases to the amount of PP1.
PP1 Binding (bound) of phosphoThr34
3) Confidence 0.00 Published 2006 Journal PLoS Computational Biology Section Body Doc Link PMC1562452 Disease Relevance 0 Pain Relevance 0
No qualitative changes in the results are seen if the dephosphorylation rate is decreased 50% when phosphoThr34 is bound to PP1.
PP1 Binding (bound) of phosphoThr34
4) Confidence 0.00 Published 2006 Journal PLoS Computational Biology Section Body Doc Link PMC1562452 Disease Relevance 0 Pain Relevance 0

General Comments

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