INT272003

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Context Info
Confidence 0.18
First Reported 2008
Last Reported 2008
Negated 0
Speculated 0
Reported most in Body
Documents 1
Total Number 6
Disease Relevance 1.10
Pain Relevance 0.07

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 (Mus musculus)
Tsc1 (Mus musculus)
Pain Link Frequency Relevance Heat
adenocard 6 67.20 Quite High
cerebral cortex 6 5.00 Very Low Very Low Very Low
transdermal 6 5.00 Very Low Very Low Very Low
Angina 6 5.00 Very Low Very Low Very Low
Disease Link Frequency Relevance Heat
Disease 126 98.00 Very High Very High Very High
Cancer 120 86.08 High High
Papillomavirus Infection 6 75.12 Quite High
Death 24 69.60 Quite High
Congenital Anomalies 18 61.84 Quite High
Apoptosis 18 61.28 Quite High
Tuberous Sclerosis 66 50.00 Quite Low
Syndrome 12 49.20 Quite Low
Polycystic Kidney Disease 36 42.60 Quite Low
Hamartoma 48 33.60 Quite Low

Sentences Mentioned In

Key: Protein Mutation Event Anatomy Negation Speculation Pain term Disease term
Detection of a ternary complex of tuberin, hamartin and 14-3-3 suggests that the tuberin-14-3-3 interaction is compatible with tuberin-hamartin binding and that 14-3-3 proteins interact with the tuberin-hamartin complex [84, 85].
tuberin Binding (binding) of hamartin
1) Confidence 0.18 Published 2008 Journal Current Genomics Section Body Doc Link PMC2691673 Disease Relevance 0.13 Pain Relevance 0.03
The hamartin/tuberin heterodimeric complex formation provides a tentative explanation for the similar disease phenotype in TSC patients with mutations in either of the two TSC genes.
tuberin Binding (formation) of hamartin associated with disease
2) Confidence 0.18 Published 2008 Journal Current Genomics Section Body Doc Link PMC2691673 Disease Relevance 0.36 Pain Relevance 0
Detection of a ternary complex of tuberin, hamartin and 14-3-3 suggests that the tuberin-14-3-3 interaction is compatible with tuberin-hamartin binding and that 14-3-3 proteins interact with the tuberin-hamartin complex [84, 85].
tuberin Binding (binding) of hamartin
3) Confidence 0.18 Published 2008 Journal Current Genomics Section Body Doc Link PMC2691673 Disease Relevance 0.13 Pain Relevance 0.03
The R611Q, R611W, A614D, C696Y and V769E substitutions [51] disrupted the tuberin–hamartin interaction, and prevented the phosphorylation of tuberin by PKB, the inhibition of S6 and S6K phosphorylation, and the stimulation of Rheb GTPase activity, cause TSC because they result in major conformational changes to tuberin.
tuberin Binding (interaction) of hamartin
4) Confidence 0.18 Published 2008 Journal Current Genomics Section Body Doc Link PMC2691673 Disease Relevance 0.06 Pain Relevance 0
The hamartin/tuberin heterodimeric complex formation provides a tentative explanation for the similar disease phenotype in TSC patients with mutations in either of the two TSC genes.
tuberin Binding (formation) of hamartin associated with disease
5) Confidence 0.18 Published 2008 Journal Current Genomics Section Body Doc Link PMC2691673 Disease Relevance 0.36 Pain Relevance 0
The R611Q, R611W, A614D, C696Y and V769E substitutions [51] disrupted the tuberin–hamartin interaction, and prevented the phosphorylation of tuberin by PKB, the inhibition of S6 and S6K phosphorylation, and the stimulation of Rheb GTPase activity, cause TSC because they result in major conformational changes to tuberin.
tuberin Binding (interaction) of hamartin
6) Confidence 0.18 Published 2008 Journal Current Genomics Section Body Doc Link PMC2691673 Disease Relevance 0.06 Pain Relevance 0

General Comments

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