INT234206

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Context Info
Confidence 0.68
First Reported 2007
Last Reported 2010
Negated 0
Speculated 0
Reported most in Body
Documents 4
Total Number 4
Disease Relevance 2.89
Pain Relevance 0.06

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)
Anatomy Link Frequency
body 1
HSP90AA1 (Homo sapiens)
Pain Link Frequency Relevance Heat
metalloproteinase 28 72.76 Quite High
antagonist 1 55.12 Quite High
chemokine 9 5.00 Very Low Very Low Very Low
cytokine 5 5.00 Very Low Very Low Very Low
Nerve growth factor 4 5.00 Very Low Very Low Very Low
Inflammation 3 5.00 Very Low Very Low Very Low
Potency 3 5.00 Very Low Very Low Very Low
Pain 2 5.00 Very Low Very Low Very Low
palliative 1 5.00 Very Low Very Low Very Low
anesthesia 1 5.00 Very Low Very Low Very Low
Disease Link Frequency Relevance Heat
Lung Cancer 137 100.00 Very High Very High Very High
Shock 32 100.00 Very High Very High Very High
Myeloid Leukemia 25 93.20 High High
Cancer 127 89.36 High High
Breast Cancer 37 85.72 High High
Reprotox - General 1 3 74.12 Quite High
Death 11 68.08 Quite High
Apoptosis 57 67.32 Quite High
Disease 18 59.60 Quite High
Stress 21 53.04 Quite High

Sentences Mentioned In

Key: Protein Mutation Event Anatomy Negation Speculation Pain term Disease term
The authors identified several proteins that are secreted by MM cells in vitro, including MHC class I antigens, heat shock proteins (HSC70, HSP90), and cytoskeletal proteins (ezrin, actinin-4) (Hegmans, 2004).
Localization (secreted) of HSP90 associated with lung cancer and shock
1) Confidence 0.68 Published 2007 Journal Biomarker Insights Section Body Doc Link PMC2717840 Disease Relevance 1.27 Pain Relevance 0.04
HSP90 inhibitors affect AKT activity indirectly through depletion of upstream signaling molecules (for example, ERBB family members) and directly by preventing HSP90-dependent conformational stability of AKT [17,21,22].
Localization (stability) of HSP90-dependent
2) Confidence 0.46 Published 2008 Journal Breast Cancer Res Section Body Doc Link PMC2397535 Disease Relevance 0.59 Pain Relevance 0.03
Our hypothesis that HNE modification of Hsp70 or Hsp90 leads to the release and activation of HSF1 is supported by a reasonable body of in vitro and in vivo results.19,27–29,40,41 However, it is also possible that modification of other cellular proteins leads to their unfolding, which attracts Hsp90 away from HSF1.
Localization (modification) of Hsp90 in body
3) Confidence 0.33 Published 2010 Journal Accounts of Chemical Research Section Body Doc Link PMC2873822 Disease Relevance 0.53 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].
Localization (Acetylation) of Hsp90
4) Confidence 0.15 Published 2010 Journal Invest New Drugs Section Body Doc Link PMC3003795 Disease Relevance 0.50 Pain Relevance 0

General Comments

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