INT272472

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Context Info
Confidence 0.72
First Reported 2008
Last Reported 2010
Negated 0
Speculated 0
Reported most in Body
Documents 2
Total Number 3
Disease Relevance 1.05
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.

cytosol (Dmpk) mitochondrion (Dmpk) endoplasmic reticulum (Dmpk)
plasma membrane (Dmpk) nucleus (Dmpk) kinase activity (Dmpk)
Anatomy Link Frequency
muscle cells 1
Dmpk (Mus musculus)
Pain Link Frequency Relevance Heat
cytokine 4 5.00 Very Low Very Low Very Low
Central nervous system 4 5.00 Very Low Very Low Very Low
spastic colon 2 5.00 Very Low Very Low Very Low
depression 2 5.00 Very Low Very Low Very Low
Kinase C 2 5.00 Very Low Very Low Very Low
Inflammation 2 5.00 Very Low Very Low Very Low
tolerance 1 5.00 Very Low Very Low Very Low
abdominal pain 1 5.00 Very Low Very Low Very Low
Disease Link Frequency Relevance Heat
Targeted Disruption 46 99.96 Very High Very High Very High
Myotonic Dystrophy 52 77.80 Quite High
Stress 2 62.96 Quite High
Cataract 18 61.32 Quite High
Arrhythmias 2 Under Development 5 60.88 Quite High
Hypopituitarism 11 59.76 Quite High
Frailty 17 59.36 Quite High
Disease 39 50.00 Quite Low
Toxicity 34 5.00 Very Low Very Low Very Low
Myotonia 28 5.00 Very Low Very Low Very Low

Sentences Mentioned In

Key: Protein Mutation Event Anatomy Negation Speculation Pain term Disease term
Although there are several predicted sites for the phosphorylation of CUGBP1 by PKC, additional studies are needed to identify phosphorylation sites for PKC and DMPK kinases within the CUGBP1 molecule.
Phosphorylation (phosphorylation) of DMPK
1) Confidence 0.72 Published 2010 Journal Current Genomics Section Body Doc Link PMC2874224 Disease Relevance 0.20 Pain Relevance 0
Mutant DMPK-mediated effect on subcellular localization, and defective phosphorylation of cytoplasmic CUG-BP1, have additionally been linked to defective translation of p21 and MEF2A in DM1, possibly explaining delayed differentiation of DM1 muscle cells.
Phosphorylation (phosphorylation) of DMPK in muscle cells
2) Confidence 0.58 Published 2008 Journal Current Genomics Section Abstract Doc Link PMC2694559 Disease Relevance 0.44 Pain Relevance 0
Examination of CUGBP1 phosphorylation status in the DMPK knock out mice suggested that CUGBP1 is a possible substrate for DMPK kinase [86].
Phosphorylation (phosphorylation) of DMPK associated with targeted disruption
3) Confidence 0.48 Published 2010 Journal Current Genomics Section Body Doc Link PMC2874224 Disease Relevance 0.40 Pain Relevance 0

General Comments

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