INT276006

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Context Info
Confidence 0.70
First Reported 2009
Last Reported 2009
Negated 0
Speculated 0
Reported most in Body
Documents 1
Total Number 8
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.

signal transduction (Pde1b) nucleus (Pde1b) cytoplasm (Pde1b)
Pde1b (Mus musculus)
Pain Link Frequency Relevance Heat
gABA 88 5.00 Very Low Very Low Very Low
depression 72 5.00 Very Low Very Low Very Low
imagery 40 5.00 Very Low Very Low Very Low
long-term potentiation 32 5.00 Very Low Very Low Very Low
Central nervous system 16 5.00 Very Low Very Low Very Low
interneuron 8 5.00 Very Low Very Low Very Low
Kinase C 8 5.00 Very Low Very Low Very Low
Dopamine 8 5.00 Very Low Very Low Very Low
Serotonin 8 5.00 Very Low Very Low Very Low
antagonist 8 5.00 Very Low Very Low Very Low
Disease Link Frequency Relevance Heat
Depression 72 5.00 Very Low Very Low Very Low
Adhesions 16 5.00 Very Low Very Low Very Low

Sentences Mentioned In

Key: Protein Mutation Event Anatomy Negation Speculation Pain term Disease term
As the amount of active CaMKII increased, active PP-1 decreased in a manner depending on PDE1 phosphorylation by CaMKII (Figure 5F).
Phosphorylation (phosphorylation) of PDE1
1) Confidence 0.70 Published 2009 Journal Mol Syst Biol Section Body Doc Link PMC2710870 Disease Relevance 0 Pain Relevance 0
The rate of PDE1 phosphorylation determined the working range within which a change of the CaMKII activity effectively influenced the PP-1 activity.
Phosphorylation (phosphorylation) of PDE1
2) Confidence 0.70 Published 2009 Journal Mol Syst Biol Section Body Doc Link PMC2710870 Disease Relevance 0 Pain Relevance 0
Figure 5B shows the strength of CaMKII autophosphorylation and that of PDE1 phosphorylation required to maintain certain levels of CaMKII activity after the transient [Ca2+]i stimulation.
Phosphorylation (phosphorylation) of PDE1
3) Confidence 0.70 Published 2009 Journal Mol Syst Biol Section Body Doc Link PMC2710870 Disease Relevance 0 Pain Relevance 0
Similarly, weakening or strengthening the PDE1 phosphorylation narrowed the range for Ca2+-dependent state switching of the CaMKII activity (Figure 5D).
Phosphorylation (phosphorylation) of PDE1
4) Confidence 0.70 Published 2009 Journal Mol Syst Biol Section Body Doc Link PMC2710870 Disease Relevance 0 Pain Relevance 0
To elucidate the role of PDE1 inhibition by CaMKII, we analyzed how the CaMKII activity affects the PP-1 activity through PDE1 phosphorylation.
Phosphorylation (phosphorylation) of PDE1
5) Confidence 0.70 Published 2009 Journal Mol Syst Biol Section Body Doc Link PMC2710870 Disease Relevance 0 Pain Relevance 0
Our model showed that synergistic action of two positive-feedback reactions, the CaMKII autophosphorylation at Thr286/287 and the negative regulation of PDE1 by CaMKII, is critical for the sustained CaMKII activation.
Phosphorylation (autophosphorylation) of PDE1
6) Confidence 0.54 Published 2009 Journal Mol Syst Biol Section Body Doc Link PMC2710870 Disease Relevance 0 Pain Relevance 0
Thus, the activity level of CaMKII seemed to mainly rely on the CaMKII autophosphorylation rather than PDE1 inhibition.
Phosphorylation (autophosphorylation) of PDE1
7) Confidence 0.54 Published 2009 Journal Mol Syst Biol Section Body Doc Link PMC2710870 Disease Relevance 0 Pain Relevance 0
The sustained CaMKII activation depended on synergistic actions of two positive-feedback reactions, CaMKII autophosphorylation and CaMKII-mediated inhibition of a CaM-dependent phosphodiesterase, PDE1.
Phosphorylation (autophosphorylation) of PDE1
8) Confidence 0.24 Published 2009 Journal Mol Syst Biol Section Abstract Doc Link PMC2710870 Disease Relevance 0 Pain Relevance 0

General Comments

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