INT234209

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Context Info
Confidence 0.54
First Reported 2008
Last Reported 2010
Negated 0
Speculated 0
Reported most in Body
Documents 5
Total Number 5
Disease Relevance 2.67
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.

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
Potency 9 5.00 Very Low Very Low Very Low
antagonist 4 5.00 Very Low Very Low Very Low
cytokine 3 5.00 Very Low Very Low Very Low
anesthesia 3 5.00 Very Low Very Low Very Low
imagery 3 5.00 Very Low Very Low Very Low
headache 3 5.00 Very Low Very Low Very Low
palliative 1 5.00 Very Low Very Low Very Low
Nicotine 1 5.00 Very Low Very Low Very Low
Inflammation 1 5.00 Very Low Very Low Very Low
pruritus 1 5.00 Very Low Very Low Very Low
Disease Link Frequency Relevance Heat
Shock 25 99.82 Very High Very High Very High
Myeloid Leukemia 25 99.02 Very High Very High Very High
Cancer 195 87.36 High High
Immunotherapy Of Cancer 3 87.20 High High
Stress 1 81.04 Quite High
Breast Cancer 169 80.80 Quite High
Advanced Or Metastatic Breast Cancer 19 73.04 Quite High
Aggression 1 58.04 Quite High
Apoptosis 30 54.60 Quite High
Body Weight 18 53.96 Quite High

Sentences Mentioned In

Key: Protein Mutation Event Anatomy Negation Speculation Pain term Disease term
The classic method of following the cellular activity of HSP90 inhibitors is through the proteasome-dependent degradation of HSP90 client proteins such as ERBB2 and AKT and the concomitant loss of signaling through the affected pathways as determined by, for example, decreased AKT phosphorylation.
Protein_catabolism (degradation) of HSP90
1) Confidence 0.54 Published 2008 Journal Breast Cancer Res Section Body Doc Link PMC2397535 Disease Relevance 0.42 Pain Relevance 0
HSP90 inhibitors cause pleiotropic effects through degradation of a large number of client proteins as well as induction of a heat shock response [32].
Protein_catabolism (degradation) of HSP90 associated with shock
2) Confidence 0.54 Published 2008 Journal Breast Cancer Res Section Body Doc Link PMC2397535 Disease Relevance 0.63 Pain Relevance 0
The classic method of following the cellular activity of HSP90 inhibitors is through the proteasome-dependent degradation of HSP90 client proteins such as ERBB2 and AKT and the concomitant loss of signaling through the affected pathways as determined by, for example, decreased AKT phosphorylation.
Protein_catabolism (degradation) of HSP90
3) Confidence 0.54 Published 2008 Journal Breast Cancer Res Section Body Doc Link PMC2397535 Disease Relevance 0.41 Pain Relevance 0
Reduction of BCR-ABL levels post-HDACi treatment, observed in most cases of HDACi treated CML cells, appears to be a consequence of disrupted Hsp90 chaperone function and proteosomal degradation of BCR-ABL [12, 65, 67, 76].
Protein_catabolism (degradation) of Hsp90 associated with myeloid leukemia
4) Confidence 0.17 Published 2010 Journal Invest New Drugs Section Body Doc Link PMC3003795 Disease Relevance 0.55 Pain Relevance 0
and its intracellular signaling.Heat shock protein Hsp90-associated signal inhibitors, which induce degradation
Protein_catabolism (degradation) of Hsp90-associated associated with shock
5) Confidence 0.06 Published 2009 Journal Journal of Oncology Section Body Doc Link PMC2668926 Disease Relevance 0.65 Pain Relevance 0

General Comments

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