INT271936

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Context Info
Confidence 0.73
First Reported 2008
Last Reported 2010
Negated 0
Speculated 0
Reported most in Body
Documents 4
Total Number 5
Disease Relevance 1.76
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 (Tsc1) embryo development (Tsc1) protein complex (Tsc1)
cytoplasm (Tsc1)
Tsc1 (Mus musculus)
Pain Link Frequency Relevance Heat
cerebral cortex 3 5.00 Very Low Very Low Very Low
transdermal 3 5.00 Very Low Very Low Very Low
adenocard 3 5.00 Very Low Very Low Very Low
Angina 3 5.00 Very Low Very Low Very Low
carbamazepine 2 5.00 Very Low Very Low Very Low
Clonidine 2 5.00 Very Low Very Low Very Low
Substantia nigra 2 5.00 Very Low Very Low Very Low
antagonist 2 5.00 Very Low Very Low Very Low
Disease Link Frequency Relevance Heat
Tuberous Sclerosis 35 100.00 Very High Very High Very High
Dna Damage 2 93.76 High High
Cancer 68 89.32 High High
Disease 93 89.00 High High
Starvation 12 88.32 High High
Apoptosis 19 82.00 Quite High
Hamartoma 24 69.96 Quite High
Death 20 68.56 Quite High
Papillomavirus Infection 3 59.92 Quite High
Stress 14 55.28 Quite High

Sentences Mentioned In

Key: Protein Mutation Event Anatomy Negation Speculation Pain term Disease term
Cdk1 phosphorylates hamartin at several sites, of which the phosphorylation at T310 regulates its interaction with Plk1 [43].
Phosphorylation (phosphorylates) of hamartin
1) Confidence 0.73 Published 2008 Journal Current Genomics Section Body Doc Link PMC2691673 Disease Relevance 0.30 Pain Relevance 0
Phosphorylation of several sites on TSC1–2 stimulates the GAP function of TSC2, whereas phosphorylation of other sites inhibits it [37, 73, 91, 92].
Phosphorylation (Phosphorylation) of TSC1
2) Confidence 0.73 Published 2008 Journal Current Genomics Section Body Doc Link PMC2691673 Disease Relevance 0.31 Pain Relevance 0
Cdk1 phosphorylates hamartin at several sites, of which the phosphorylation at T310 regulates its interaction with Plk1 [43].
Phosphorylation (phosphorylation) of hamartin
3) Confidence 0.56 Published 2008 Journal Current Genomics Section Body Doc Link PMC2691673 Disease Relevance 0.30 Pain Relevance 0
phosphatase) and TSC1 which inhibits mTOR.
Phosphorylation (phosphatase) of TSC1
4) Confidence 0.30 Published 2010 Journal Seminars in Cell & Developmental Biology Section Body Doc Link PMC2938570 Disease Relevance 0.68 Pain Relevance 0
The phosphorylation-dependent Akt activation results in the phosphorylation of a host of other proteins, including the tuberous sclerosis complex 1/2 (TSC1/TSC2).
Phosphorylation (phosphorylation) of TSC1 associated with tuberous sclerosis
5) Confidence 0.30 Published 2010 Journal Seminars in Cell & Developmental Biology Section Body Doc Link PMC2938570 Disease Relevance 0.17 Pain Relevance 0

General Comments

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