INT271938

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Context Info
Confidence 0.43
First Reported 2008
Last Reported 2008
Negated 0
Speculated 0
Reported most in Body
Documents 1
Total Number 12
Disease Relevance 3.18
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 (Tsc1) embryo development (Tsc1) protein complex (Tsc1)
cytoplasm (Tsc1)
Anatomy Link Frequency
neuronal 1
reticulum 1
Tsc1 (Mus musculus)
Pain Link Frequency Relevance Heat
adenocard 12 71.36 Quite High
cerebral cortex 12 5.00 Very Low Very Low Very Low
transdermal 12 5.00 Very Low Very Low Very Low
Angina 12 5.00 Very Low Very Low Very Low
Disease Link Frequency Relevance Heat
Apoptosis 36 99.28 Very High Very High Very High
Death 48 98.40 Very High Very High Very High
Cancer 240 98.32 Very High Very High Very High
Disease 252 98.00 Very High Very High Very High
Hamartoma 96 97.16 Very High Very High Very High
Stress 24 96.64 Very High Very High Very High
Syndrome 24 90.36 High High
Polycystic Kidney Disease 72 83.76 Quite High
Papillomavirus Infection 12 82.80 Quite High
Congenital Anomalies 36 61.52 Quite High

Sentences Mentioned In

Key: Protein Mutation Event Anatomy Negation Speculation Pain term Disease term
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.
hamartin Binding (interaction) of
1) Confidence 0.43 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.
hamartin Binding (formation) of associated with disease
2) Confidence 0.43 Published 2008 Journal Current Genomics Section Body Doc Link PMC2691673 Disease Relevance 0.36 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.
hamartin Binding (binding) of
3) Confidence 0.37 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.
hamartin Binding (complex) of
4) Confidence 0.33 Published 2008 Journal Current Genomics Section Body Doc Link PMC2691673 Disease Relevance 0.13 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].
hamartin Binding (binding) of
5) Confidence 0.33 Published 2008 Journal Current Genomics Section Body Doc Link PMC2691673 Disease Relevance 0.13 Pain Relevance 0.03
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.
TSC1 Binding (loss) of in reticulum associated with stress and cancer
6) Confidence 0.33 Published 2008 Journal Current Genomics Section Body Doc Link PMC2691673 Disease Relevance 0.54 Pain Relevance 0
Hamartin binds to NADE with its coiled coil domain domain.
Hamartin Binding (binds) of
7) Confidence 0.33 Published 2008 Journal Current Genomics Section Body Doc Link PMC2691673 Disease Relevance 0.44 Pain Relevance 0
Hamartin has also been shown to interact with neurofilament-L [33].
Hamartin Binding (interact) of
8) Confidence 0.32 Published 2008 Journal Current Genomics Section Body Doc Link PMC2691673 Disease Relevance 0 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.
hamartin Binding (binding) of
9) Confidence 0.29 Published 2008 Journal Current Genomics Section Body Doc Link PMC2691673 Disease Relevance 0.31 Pain Relevance 0
Down-regulation of hamartin with TSC1 siRNA led to failure of NGF-induced apoptosis in PC12h cells suggesting that the association of hamartin with NADE is involved in neuronal cell death, which could explain why hamartoma cells are not eliminated in TSC.
hamartin Binding (association) of in neuronal associated with hamartoma, apoptosis and death
10) Confidence 0.29 Published 2008 Journal Current Genomics Section Body Doc Link PMC2691673 Disease Relevance 0.47 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].
hamartin Binding (complex) of
11) Confidence 0.29 Published 2008 Journal Current Genomics Section Body Doc Link PMC2691673 Disease Relevance 0.11 Pain Relevance 0.04
Hamartin has been reported to interact with Plk1 and to be localized to the centrosome.
Hamartin Binding (interact) of
12) Confidence 0.28 Published 2008 Journal Current Genomics Section Body Doc Link PMC2691673 Disease Relevance 0.32 Pain Relevance 0

General Comments

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