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Context Info
Confidence 0.63
First Reported 2008
Last Reported 2010
Negated 0
Speculated 0
Reported most in Abstract
Documents 4
Total Number 4
Disease Relevance 0.83
Pain Relevance 1.01

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 (IGF1) extracellular space (IGF1) extracellular region (IGF1)
IGF1 (Homo sapiens)
Pain Link Frequency Relevance Heat
bDMF 10 96.56 Very High Very High Very High
opioid receptor 6 94.08 High High
Enkephalin 2 86.32 High High
agonist 8 84.56 Quite High
MU agonist 2 75.00 Quite High
Limbic system 1 68.92 Quite High
Neuronal excitability 1 64.16 Quite High
Hippocampus 11 17.08 Low Low
Glutamate receptor 2 12.84 Low Low
tetrodotoxin 3 11.88 Low Low
Disease Link Frequency Relevance Heat
Diabetes Mellitus 2 93.92 High High
Motor Neuron Diseases 1 89.84 High High
Stress 2 85.20 High High
Neuroblastoma 4 82.68 Quite High
Laron Syndrome 15 69.76 Quite High
Convulsion 30 50.00 Quite Low
Nutritional Deficiencies 5 43.04 Quite Low
Liver Disease 2 41.92 Quite Low
Epilepsy 22 5.00 Very Low Very Low Very Low
Hypoglycemia 13 5.00 Very Low Very Low Very Low

Sentences Mentioned In

Key: Protein Mutation Event Anatomy Negation Speculation Pain term Disease term
Another recombinant form of IGF-1 was developed by Chiron Corp (Emeryville, CA, USA) in collaboration with Cephalon Inc.
Phosphorylation (form) of IGF-1
1) Confidence 0.63 Published 2009 Journal Therapeutics and Clinical Risk Management Section Body Doc Link PMC2724186 Disease Relevance 0.43 Pain Relevance 0
Silencing of beta-arrestin 2 uncouples the crosstalk between the two receptors, thus maintaining IGF-I-mediated receptor phosphorylation and ERK 1/2 activation even after prolonged DAMGO exposure.
Phosphorylation (phosphorylation) of IGF-I-mediated
2) Confidence 0.14 Published 2010 Journal FEBS Lett. Section Abstract Doc Link 20643133 Disease Relevance 0.15 Pain Relevance 0.32
Brief (15 min) but not prolonged exposure to DAMGO transregulates the insulin-like growth factor-I (IGF-I) receptor, as evidenced by its phosphorylation in the absence of IGF-I.
Phosphorylation (phosphorylation) of IGF-I
3) Confidence 0.11 Published 2010 Journal FEBS Lett. Section Abstract Doc Link 20643133 Disease Relevance 0.16 Pain Relevance 0.33
Tyrosine phosphorylation of KCC2 by insulin-like growth factor (IGF-1) and tyrosine kinases increase its activity [144].
Phosphorylation (phosphorylation) of insulin-like growth factor
4) Confidence 0.03 Published 2008 Journal Current Neuropharmacology Section Body Doc Link PMC2645547 Disease Relevance 0.09 Pain Relevance 0.36

General Comments

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