INT271914

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Context Info
Confidence 0.38
First Reported 2008
Last Reported 2010
Negated 0
Speculated 0
Reported most in Body
Documents 5
Total Number 7
Disease Relevance 3.08
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 (Tsc1) embryo development (Tsc1) protein complex (Tsc1)
cytoplasm (Tsc1)
Anatomy Link Frequency
brain 1
reticulum 1
Tsc1 (Mus musculus)
Pain Link Frequency Relevance Heat
transdermal 4 71.08 Quite High
Angina 4 14.16 Low Low
cerebral cortex 4 5.00 Very Low Very Low Very Low
adenocard 4 5.00 Very Low Very Low Very Low
carbamazepine 3 5.00 Very Low Very Low Very Low
Clonidine 3 5.00 Very Low Very Low Very Low
Substantia nigra 3 5.00 Very Low Very Low Very Low
antagonist 3 5.00 Very Low Very Low Very Low
Disease Link Frequency Relevance Heat
Hamartoma 32 98.58 Very High Very High Very High
Anaplastic Astrocytoma 24 98.54 Very High Very High Very High
Cancer 92 98.32 Very High Very High Very High
Convulsion 36 98.32 Very High Very High Very High
Stress 20 96.64 Very High Very High Very High
Epilepsy 24 95.60 Very High Very High Very High
Encephalopathy 4 95.20 Very High Very High Very High
Death 28 94.00 High High
Tuberous Sclerosis 47 92.68 High High
Congenital Anomalies 12 92.12 High 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.
Negative_regulation (loss) of TSC1 in reticulum associated with stress and cancer
1) Confidence 0.38 Published 2008 Journal Current Genomics Section Body Doc Link PMC2691673 Disease Relevance 0.54 Pain Relevance 0
Zeng et al. [125] recently demonstrated that rapamycin has strong efficacy for preventing seizures and prolonging survival in Tsc1GFAPCKO mice, a mouse model of TSC with conditional inactivation of the Tsc1 gene in glial fibrillary acidic protein (GFAP)–positive cells (Tsc1GFAPCKO mice), which develops progressive epilepsy, encephalopathy, and premature death, as well as cellular and molecular brain abnormalities likely contributing to epileptogenesis.


Negative_regulation (inactivation) of Tsc1 in brain associated with epilepsy, convulsion, congenital anomalies, encephalopathy and death
2) Confidence 0.38 Published 2008 Journal Current Genomics Section Body Doc Link PMC2691673 Disease Relevance 1.04 Pain Relevance 0.04
On the other hand, recent evidence suggests that both tuber giant cells and SEGA cells have similar immunophenotypes, and SEGAs commonly sustain two-hit inactivation of either TSC1 or TSC2.
Negative_regulation (inactivation) of TSC1 associated with anaplastic astrocytoma
3) Confidence 0.38 Published 2008 Journal Current Genomics Section Body Doc Link PMC2691673 Disease Relevance 0.40 Pain Relevance 0
For many years, the prevailing model has been that the hamartomas of TSC develop through a two-hit mechanism in which there is complete loss of expression of functional TSC1 or TSC2, supported by findings of loss of heterozygosity (LOH) in TSC tumour samples [23-26].
Negative_regulation (loss) of TSC1 associated with cancer and hamartoma
4) Confidence 0.38 Published 2008 Journal Current Genomics Section Body Doc Link PMC2691673 Disease Relevance 0.44 Pain Relevance 0
Since TSC1/TSC2 acts as the GTPase-activating protein (GAP) for the Ras-family GTP binding protein, Rheb, which directly binds and activates mTOR [17], loss of TSC1/TSC2 activity results in mTOR activation.
Negative_regulation (loss) of TSC1
5) Confidence 0.21 Published 2010 Journal Seminars in Cell & Developmental Biology Section Body Doc Link PMC2938570 Disease Relevance 0.32 Pain Relevance 0
Phosphorylation of TSC2 by these kinases leads to the disruption of the heterodimer with TSC1, resulting in loss of TSC1/TSC2 activity.
Negative_regulation (loss) of TSC1
6) Confidence 0.21 Published 2010 Journal Seminars in Cell & Developmental Biology Section Body Doc Link PMC2938570 Disease Relevance 0.20 Pain Relevance 0
Phosphorylation of TSC2 by these kinases leads to the disruption of the heterodimer with TSC1, resulting in loss of TSC1/TSC2 activity.
Negative_regulation (disruption) of TSC1
7) Confidence 0.16 Published 2010 Journal Seminars in Cell & Developmental Biology Section Body Doc Link PMC2938570 Disease Relevance 0.15 Pain Relevance 0

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