INT192235

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Context Info
Confidence 0.19
First Reported 2006
Last Reported 2010
Negated 0
Speculated 0
Reported most in Body
Documents 6
Total Number 8
Disease Relevance 1.46
Pain Relevance 0.60

This is a graph with borders and nodes. Maybe there is an Imagemap used so the nodes may be linking to some Pages.

unfolded protein binding (Hsp90aa1) protein folding (Hsp90aa1) cytosol (Hsp90aa1)
ATPase activity (Hsp90aa1) intracellular (Hsp90aa1) response to stress (Hsp90aa1)
Anatomy Link Frequency
artery endothelium 1
proximal 1
Hsp90aa1 (Mus musculus)
Pain Link Frequency Relevance Heat
corticosteroid 294 99.40 Very High Very High Very High
Neurotransmitter 13 78.56 Quite High
Neuronal excitability 12 54.32 Quite High
Inflammation 5 54.12 Quite High
Pain 4 53.60 Quite High
midbrain 24 49.12 Quite Low
Potency 4 40.76 Quite Low
Pyramidal cell 3 39.28 Quite Low
amygdala 18 22.08 Low Low
Hippocampus 66 5.00 Very Low Very Low Very Low
Disease Link Frequency Relevance Heat
Shock 58 100.00 Very High Very High Very High
Cancer 11 98.76 Very High Very High Very High
Muscular Atrophy 3 80.16 Quite High
Manic Depressive Disorder 19 79.00 Quite High
Stress 181 64.12 Quite High
Cataract 3 57.12 Quite High
Mycobacterium Infection 1 56.00 Quite High
INFLAMMATION 5 54.12 Quite High
Vasculitis 2 52.56 Quite High
Clinical Trials And Case Reports 3 50.00 Quite Low

Sentences Mentioned In

Key: Protein Mutation Event Anatomy Negation Speculation Pain term Disease term
Fkbp6 forms a complex with Gapdh and Hsp90, inhibiting and down regulating Gapdh, but the function of Hsp90 in this complex has not been elucidated [48].
Hsp90 Binding (complex) of
1) Confidence 0.19 Published 2010 Journal PLoS ONE Section Body Doc Link PMC2965669 Disease Relevance 0.13 Pain Relevance 0
Fkbp6 forms a complex with Gapdh and Hsp90, inhibiting and down regulating Gapdh, but the function of Hsp90 in this complex has not been elucidated [48].
Hsp90 Binding (complex) of
2) Confidence 0.19 Published 2010 Journal PLoS ONE Section Body Doc Link PMC2965669 Disease Relevance 0.13 Pain Relevance 0
Hspabp, thought to be a tumor suppressor, is important for Hsp70 function by mediating its interaction with Hsp90 [86].
Hsp90 Binding (interaction) of associated with cancer
3) Confidence 0.18 Published 2010 Journal PLoS ONE Section Body Doc Link PMC2965669 Disease Relevance 0.36 Pain Relevance 0
It has been shown that an HSP90 inhibitor, geldanamycin, can bind to GRP94, inhibit its function, and increase the transcription of ER molecular chaperones [24].
HSP90 Binding (bind) of
4) Confidence 0.13 Published 2009 Journal PLoS ONE Section Body Doc Link PMC2607540 Disease Relevance 0.34 Pain Relevance 0
In addition, hsp90 interactions with MEK2, another kinase upstream of MAPK, has been shown to mediate MAPK pathway activation by estradiol [83].
hsp90 Binding (interactions) of
5) Confidence 0.11 Published 2010 Journal Mol Brain Section Body Doc Link PMC2841592 Disease Relevance 0.09 Pain Relevance 0.21
Many unliganded nuclear receptors (e.g. nGR), are tethered in the cytoplasm through their association with chaperone proteins such as heat shock protein 90 (hsp90); this complex is dissociated upon arrival of the ligand [24].
hsp90 Binding (association) of associated with shock
6) Confidence 0.09 Published 2010 Journal Mol Brain Section Body Doc Link PMC2841592 Disease Relevance 0.10 Pain Relevance 0.13
Interestingly, hsp90 is known to interact with src kinase [82], a membrane-proximal kinase thought to mediate the rapid activation of the MAPK pathway by corticosteroids.
hsp90 Binding (interact) of in proximal associated with corticosteroid
7) Confidence 0.09 Published 2010 Journal Mol Brain Section Body Doc Link PMC2841592 Disease Relevance 0.10 Pain Relevance 0.17
NO is also instrumental in promoting Ang1-induced angiogenesis in combination with HSP90 and Akt in coronary artery endothelium [12].
HSP90 Binding (combination) of in artery endothelium
8) Confidence 0.04 Published 2006 Journal BMC Cell Biol Section Body Doc Link PMC1456963 Disease Relevance 0.23 Pain Relevance 0.08

General Comments

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