INT228895

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Context Info
Confidence 0.30
First Reported 2008
Last Reported 2008
Negated 0
Speculated 0
Reported most in Body
Documents 5
Total Number 6
Disease Relevance 2.41
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 (Tsc2) signal transduction (Tsc2) Golgi apparatus (Tsc2)
nucleus (Tsc2) intracellular (Tsc2) protein complex (Tsc2)
Anatomy Link Frequency
reticulum 1
Tsc2 (Rattus norvegicus)
Pain Link Frequency Relevance Heat
agonist 3 5.00 Very Low Very Low Very Low
anesthesia 3 5.00 Very Low Very Low Very Low
cerebral cortex 2 5.00 Very Low Very Low Very Low
transdermal 2 5.00 Very Low Very Low Very Low
adenocard 2 5.00 Very Low Very Low Very Low
Angina 2 5.00 Very Low Very Low Very Low
Pain 1 5.00 Very Low Very Low Very Low
Disease Link Frequency Relevance Heat
Cancer 112 98.64 Very High Very High Very High
Syndrome 5 98.36 Very High Very High Very High
Stress 25 96.96 Very High Very High Very High
Leiomyosarcoma 18 95.24 Very High Very High Very High
Uterine Fibroids 7 94.60 High High
Uterine Cancer 3 92.84 High High
Polycystic Kidney Disease 12 91.76 High High
Epithelioid Leiomyoma 4 87.76 High High
Tuberous Sclerosis 24 86.36 High High
Apoptosis 12 79.12 Quite High

Sentences Mentioned In

Key: Protein Mutation Event Anatomy Negation Speculation Pain term Disease term
Ozcan et al. [98] found that loss of TSC1 or TSC2 in cell lines and mouse or human tumours caused endoplasmic reticulum (ER) stress and activated the unfolded protein response.
TSC2 Binding (loss) of in reticulum associated with stress and cancer
1) Confidence 0.30 Published 2008 Journal Current Genomics Section Body Doc Link PMC2691673 Disease Relevance 0.54 Pain Relevance 0
The C-terminal domain within the TSC2 protein was recognized as being homologous to other GAP domains when it was cloned in 1993 [30].
TSC2 Binding (recognized) of
2) Confidence 0.29 Published 2008 Journal Current Genomics Section Body Doc Link PMC2691673 Disease Relevance 0.25 Pain Relevance 0
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 (activity) of
3) Confidence 0.16 Published 2008 Journal Diabetes Section Body Doc Link PMC2551671 Disease Relevance 0.12 Pain Relevance 0
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
4) Confidence 0.16 Published 2008 Journal Diabetes Section Body Doc Link PMC2551671 Disease Relevance 0.14 Pain Relevance 0
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 (ubiquitination) of
5) Confidence 0.16 Published 2008 Journal Diabetes Section Body Doc Link PMC2551671 Disease Relevance 0.15 Pain Relevance 0
PEComas, of course, have a known association with TSC2 gene alterations [80].
TSC2 gene Binding (association) of
6) Confidence 0.10 Published 2008 Journal Int Semin Surg Oncol Section Body Doc Link PMC2278149 Disease Relevance 1.21 Pain Relevance 0

General Comments

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