INT246793

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Context Info
Confidence 0.04
First Reported 2008
Last Reported 2008
Negated 0
Speculated 0
Reported most in Body
Documents 1
Total Number 2
Disease Relevance 0.71
Pain Relevance 0.04

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

cytosol (Tsc2, Tsc1) protein complex (Tsc2, Tsc1) cytoplasm (Tsc2, Tsc1)
signal transduction (Tsc2) Golgi apparatus (Tsc2) nucleus (Tsc2)
Tsc2 (Rattus norvegicus)
Tsc1 (Rattus norvegicus)
Pain Link Frequency Relevance Heat
agonist 2 72.88 Quite High
anesthesia 2 5.00 Very Low Very Low Very Low
Disease Link Frequency Relevance Heat
Cancer 2 98.80 Very High Very High Very High
Adhesions 2 87.92 High High
Targeted Disruption 2 81.36 Quite High
Apoptosis 4 75.52 Quite High
Injury 8 65.76 Quite High
Diabetes Mellitus 78 65.36 Quite High
Diabetes Complications 2 61.84 Quite High
Albuminuria 2 60.36 Quite High
Stress 14 35.48 Quite Low
Renal Disease 4 32.60 Quite Low

Sentences Mentioned In

Key: Protein Mutation Event Anatomy Negation Speculation Pain term Disease term
Tuberin normally exists in an active state physically bound to hamartin, the product of TSC-1 gene, to form a stable complex (22).
Tuberin Binding (bound) of hamartin
1) Confidence 0.04 Published 2008 Journal Diabetes Section Body Doc Link PMC2551671 Disease Relevance 0.57 Pain Relevance 0.04
Phosphorylation of tuberin by Akt affects its function through at least two mechanisms: first, phosphorylation decreases the activity of tuberin; second, phosphorylation destabilizes tuberin by disrupting the complex formation between hamartin and tuberin, resulting in ubiquitination of free tuberin and its degradation by the proteosome (27).
tuberin Binding (formation) of hamartin
2) Confidence 0.03 Published 2008 Journal Diabetes Section Body Doc Link PMC2551671 Disease Relevance 0.14 Pain Relevance 0

General Comments

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