INT165846

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Context Info
Confidence 0.27
First Reported 2008
Last Reported 2010
Negated 0
Speculated 1
Reported most in Body
Documents 4
Total Number 5
Disease Relevance 2.19
Pain Relevance 0.58

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) small molecule metabolic process (HSP90AA1) intracellular (HSP90AA1)
response to stress (HSP90AA1) cytoplasm (HSP90AA1) cytosol (HSP90AA1)
HSP90AA1 (Homo sapiens)
Pain Link Frequency Relevance Heat
Morphine 6 97.00 Very High Very High Very High
antagonist 2 88.92 High High
Potency 6 72.96 Quite High
agonist 1 53.64 Quite High
Opioid 1 49.40 Quite Low
cytokine 3 5.00 Very Low Very Low Very Low
anesthesia 2 5.00 Very Low Very Low Very Low
Inflammation 2 5.00 Very Low Very Low Very Low
imagery 2 5.00 Very Low Very Low Very Low
palliative 1 5.00 Very Low Very Low Very Low
Disease Link Frequency Relevance Heat
Cancer 124 97.98 Very High Very High Very High
Breast Cancer 72 97.96 Very High Very High Very High
Shock 42 97.60 Very High Very High Very High
Myeloid Leukemia 25 90.64 High High
Stress 21 80.00 Quite High
Neuroblastoma 1 68.88 Quite High
Apoptosis 36 64.76 Quite High
Hematologic Neoplasms 4 63.08 Quite High
Solid Tumor 4 61.84 Quite High
Retinoblastoma 1 21.08 Low Low

Sentences Mentioned In

Key: Protein Mutation Event Anatomy Negation Speculation Pain term Disease term
In addition to ER, a number of other HSP90 client proteins have been shown to be involved in breast cancer progression such as those that are important for signaling through the phosphahtidylinositol-3-kinase (PI3K/p110?)
Regulation (number) of HSP90 associated with breast cancer
1) Confidence 0.27 Published 2008 Journal Breast Cancer Res Section Body Doc Link PMC2397535 Disease Relevance 0.74 Pain Relevance 0.04
Destabilization of the HSP90-p23 interaction in tumor cells and the subsequent measurement using immunoprecipitation therefore can be used to monitor the effect of HSP90 inhibitors on the HSP90 catalytic cycle (Figure 1b).
Regulation (effect) of HSP90 associated with cancer
2) Confidence 0.27 Published 2008 Journal Breast Cancer Res Section Body Doc Link PMC2397535 Disease Relevance 0.10 Pain Relevance 0.04
These results indicate that Hsp90 is a new pharmacological target for the suppression of adenylate cyclase sensitization induced by chronic morphine treatment.
Regulation (target) of Hsp90 associated with morphine
3) Confidence 0.16 Published 2010 Journal Biochem. Biophys. Res. Commun. Section Abstract Doc Link 20100459 Disease Relevance 0.27 Pain Relevance 0.50
We are presently determining the sites of Hsp90 and Hsp70 modification and the functional consequences of HNE modification both in terms of HSF1 binding as well as its affiliation with other specific client proteins.
Spec (determining) Regulation (modification) of Hsp90
4) Confidence 0.12 Published 2010 Journal Accounts of Chemical Research Section Body Doc Link PMC2873822 Disease Relevance 0.59 Pain Relevance 0
Acetylation of Hsp90, a HDAC6 substrate, results in accelerated degredation of HSP90 client proteins, including BCR-ABL, AKT and c-Raf, via the 26S proteosome [65, 76, 89–91].
Regulation (degredation) of HSP90
5) Confidence 0.09 Published 2010 Journal Invest New Drugs Section Body Doc Link PMC3003795 Disease Relevance 0.50 Pain Relevance 0

General Comments

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