INT323479

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Context Info
Confidence 0.06
First Reported 2010
Last Reported 2010
Negated 0
Speculated 0
Reported most in Body
Documents 1
Total Number 4
Disease Relevance 1.80
Pain Relevance 0.49

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

cytosol (Sorbs1) transport (Sorbs1) plasma membrane (Sorbs1)
cytoskeleton (Sorbs1) nucleus (Sorbs1) cytoplasm (Sorbs1)
Anatomy Link Frequency
muscle 2
fat cells 2
Sorbs1 (Mus musculus)
Pain Link Frequency Relevance Heat
Kinase C 12 99.16 Very High Very High Very High
tolerance 72 5.00 Very Low Very Low Very Low
antagonist 56 5.00 Very Low Very Low Very Low
Somatostatin 16 5.00 Very Low Very Low Very Low
vagus nerve 8 5.00 Very Low Very Low Very Low
Neurotransmitter 4 5.00 Very Low Very Low Very Low
agonist 4 5.00 Very Low Very Low Very Low
Action potential 4 5.00 Very Low Very Low Very Low
Opioid 4 5.00 Very Low Very Low Very Low
Calcium channel 4 5.00 Very Low Very Low Very Low
Disease Link Frequency Relevance Heat
Obesity 196 98.64 Very High Very High Very High
Hyperinsulinism 40 61.04 Quite High
Diabetes Mellitus 120 6.32 Low Low
Targeted Disruption 216 5.00 Very Low Very Low Very Low
Impaired Glucose Tolerance 80 5.00 Very Low Very Low Very Low
Insulin Resistance 72 5.00 Very Low Very Low Very Low
Body Weight 36 5.00 Very Low Very Low Very Low
Disease 24 5.00 Very Low Very Low Very Low
Appetite Loss 20 5.00 Very Low Very Low Very Low
Hyperglycemia 16 5.00 Very Low Very Low Very Low

Sentences Mentioned In

Key: Protein Mutation Event Anatomy Negation Speculation Pain term Disease term
Intriguingly, whereas many growth factors trigger the activation of PI3K, AKT, and PKC in many cell types, aspects of the c-Cbl–CAP pathway, including the tyrosine phosphorylation and the expression of CAP, seem to be unique to muscle and fat cells [144].
Phosphorylation (phosphorylation) of CAP in fat cells associated with kinase c and obesity
1) Confidence 0.06 Published 2010 Journal International Journal of Peptides Section Body Doc Link PMC2911604 Disease Relevance 0.45 Pain Relevance 0.12
Intriguingly, whereas many growth factors trigger the activation of PI3K, AKT, and PKC in many cell types, aspects of the c-Cbl–CAP pathway, including the tyrosine phosphorylation and the expression of CAP, seem to be unique to muscle and fat cells [144].
Phosphorylation (phosphorylation) of CAP in fat cells associated with kinase c and obesity
2) Confidence 0.05 Published 2010 Journal International Journal of Peptides Section Body Doc Link PMC2911604 Disease Relevance 0.45 Pain Relevance 0.12
Intriguingly, whereas many growth factors trigger the activation of PI3K, AKT, and PKC in many cell types, aspects of the c-Cbl–CAP pathway, including the tyrosine phosphorylation and the expression of CAP, seem to be unique to muscle and fat cells [144].
Phosphorylation (phosphorylation) of CAP in muscle associated with kinase c and obesity
3) Confidence 0.02 Published 2010 Journal International Journal of Peptides Section Body Doc Link PMC2911604 Disease Relevance 0.45 Pain Relevance 0.12
Intriguingly, whereas many growth factors trigger the activation of PI3K, AKT, and PKC in many cell types, aspects of the c-Cbl–CAP pathway, including the tyrosine phosphorylation and the expression of CAP, seem to be unique to muscle and fat cells [144].
Phosphorylation (phosphorylation) of CAP in muscle associated with kinase c and obesity
4) Confidence 0.02 Published 2010 Journal International Journal of Peptides Section Body Doc Link PMC2911604 Disease Relevance 0.45 Pain Relevance 0.12

General Comments

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