INT271941

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Context Info
Confidence 0.24
First Reported 2007
Last Reported 2008
Negated 0
Speculated 1
Reported most in Body
Documents 12
Total Number 12
Disease Relevance 2.96
Pain Relevance 0.11

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) protein complex (Tsc2) cytoplasm (Tsc2)
Tsc2 (Mus musculus)
Pain Link Frequency Relevance Heat
adenocard 11 81.32 Quite High
cerebral cortex 11 5.00 Very Low Very Low Very Low
transdermal 11 5.00 Very Low Very Low Very Low
Angina 11 5.00 Very Low Very Low Very Low
Mechanosensation 4 5.00 Very Low Very Low Very Low
Somatostatin 4 5.00 Very Low Very Low Very Low
imagery 3 5.00 Very Low Very Low Very Low
fibrosis 2 5.00 Very Low Very Low Very Low
abdominal pain 1 5.00 Very Low Very Low Very Low
Mechanotransduction 1 5.00 Very Low Very Low Very Low
Disease Link Frequency Relevance Heat
Cancer 221 100.00 Very High Very High Very High
Disease 261 98.00 Very High Very High Very High
Syndrome 26 89.28 High High
Tuberous Sclerosis 122 83.56 Quite High
Death 44 83.04 Quite High
Polycystic Kidney Disease 128 82.68 Quite High
Papillomavirus Infection 11 81.36 Quite High
Hamartoma 88 80.80 Quite High
Cyst 76 77.12 Quite High
Apoptosis 50 75.24 Quite High

Sentences Mentioned In

Key: Protein Mutation Event Anatomy Negation Speculation Pain term Disease term
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 associated with disease
1) Confidence 0.24 Published 2008 Journal Current Genomics Section Body Doc Link PMC2691673 Disease Relevance 0.36 Pain Relevance 0
The phosphorylation of tuberin by Akt and MK2 promotes the binding of tuberin with 14-3-3 proteins. 14-3-3 proteins are members of a group of proteins that specifically interact with phosphorylated proteins, facilitating the phosphorylation-dependent control of protein activity [83].
tuberin Binding (binding) of
2) Confidence 0.24 Published 2008 Journal Current Genomics Section Body Doc Link PMC2691673 Disease Relevance 0 Pain Relevance 0.04
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 (complex) of
3) Confidence 0.19 Published 2008 Journal Current Genomics Section Body Doc Link PMC2691673 Disease Relevance 0.11 Pain Relevance 0.04
The region of hamartin known to span the interacting domain with tuberin is within the amino acids 302–430, and the first 418 amino acids of tuberin contain the binding site for hamartin.
tuberin Binding (binding) of
4) Confidence 0.19 Published 2008 Journal Current Genomics Section Body Doc Link PMC2691673 Disease Relevance 0.30 Pain Relevance 0
Neither tuberin nor hamartin are in a complex with Skp2 and tuberin does not affect Skp2 protein levels, and the SCFSkp2 ubiquitin ligase does not regulate tuberin stability.
tuberin Binding (complex) of
5) Confidence 0.19 Published 2008 Journal Current Genomics Section Body Doc Link PMC2691673 Disease Relevance 0.13 Pain Relevance 0
A possible function of the interaction between 14-3-3 proteins and phosphorylated tuberin is to inhibit the formation of tuberin-hamartin complex, in order to decrease the stability of tuberin and release of the activated mTOR [84].
tuberin Binding (interaction) of
6) Confidence 0.19 Published 2008 Journal Current Genomics Section Body Doc Link PMC2691673 Disease Relevance 0.22 Pain Relevance 0.03
The observed binding of the tumour suppressor protein tuberin to the tumour suppressor protein p27 provides a molecular explanation for the effects of the TSC genes on p27 protein stability [97].
tuberin Binding (binding) of associated with cancer
7) Confidence 0.19 Published 2008 Journal Current Genomics Section Body Doc Link PMC2691673 Disease Relevance 0.46 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
8) Confidence 0.18 Published 2008 Journal Current Genomics Section Body Doc Link PMC2691673 Disease Relevance 0.06 Pain Relevance 0
The region of hamartin known to span the interacting domain with tuberin is within the amino acids 302–430, and the first 418 amino acids of tuberin contain the binding site for hamartin.
tuberin Binding (interacting) of
9) Confidence 0.18 Published 2008 Journal Current Genomics Section Body Doc Link PMC2691673 Disease Relevance 0.30 Pain Relevance 0
However, binding of tuberin to p27 sequesters p27 from Skp2 accompanied by a stabilization of the p27 interaction with cdk2, and hence, Skp2-induced p27 degradation and cell cycle progression is abolished by tuberin’s protective binding to p27.
tuberin Binding (binding) of
10) Confidence 0.18 Published 2008 Journal Current Genomics Section Body Doc Link PMC2691673 Disease Relevance 0.16 Pain Relevance 0
A recent study has demonstrated that the forkhead transcription factor FoxO is capable of binding to tuberin [90].
tuberin Binding (binding) of
11) Confidence 0.16 Published 2008 Journal Current Genomics Section Body Doc Link PMC2691673 Disease Relevance 0.37 Pain Relevance 0
Polycystin-1 appeared to form a complex with tuberin and regulate the activity of mTOR, an important regulator of protein synthesis and cellular differentiation [95].
tuberin Spec (appeared) Binding (complex) of
12) Confidence 0.09 Published 2007 Journal Cell Mol Life Sci Section Body Doc Link PMC2775119 Disease Relevance 0.50 Pain Relevance 0

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