INT278334

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Context Info
Confidence 0.30
First Reported 2009
Last Reported 2010
Negated 0
Speculated 0
Reported most in Body
Documents 3
Total Number 10
Disease Relevance 4.34
Pain Relevance 0.68

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 (Hsp90ab1) protein folding (Hsp90ab1) cytosol (Hsp90ab1)
mitochondrion (Hsp90ab1) intracellular (Hsp90ab1) response to stress (Hsp90ab1)
Anatomy Link Frequency
sensory neuron 2
Hsp90ab1 (Mus musculus)
Pain Link Frequency Relevance Heat
Demyelination 80 98.16 Very High Very High Very High
unmyelinated 56 96.84 Very High Very High Very High
diabetic neuropathy 16 81.60 Quite High
Sciatic nerve 24 80.04 Quite High
agonist 18 75.04 Quite High
hypoalgesia 32 75.00 Quite High
Potency 8 71.68 Quite High
medulla 8 65.36 Quite High
cytokine 10 53.36 Quite High
Inflammation 8 52.96 Quite High
Disease Link Frequency Relevance Heat
Shock 62 100.00 Very High Very High Very High
Diabetes Complications 24 98.60 Very High Very High Very High
Death 117 98.56 Very High Very High Very High
Demyelinating Disease 80 98.16 Very High Very High Very High
Diabetes Mellitus 320 95.88 Very High Very High Very High
Wound Healing 8 91.80 High High
Reperfusion Injury 8 90.48 High High
Insulin Resistance 16 90.00 High High
Cv Unclassified Under Development 10 89.72 High High
Targeted Disruption 28 83.68 Quite High

Sentences Mentioned In

Key: Protein Mutation Event Anatomy Negation Speculation Pain term Disease term
However, to the best of our knowledge, the potential efficacy of Hsp90 inhibitors and Hsp70 induction against other diabetic complications has not been adequately examined.
Negative_regulation (inhibitors) of Hsp90 associated with diabetes complications
1) Confidence 0.30 Published 2010 Journal ASN NEURO Section Body Doc Link PMC2919983 Disease Relevance 1.14 Pain Relevance 0.03
Although inhibiting Hsp90 can destabilize its association with client proteins such as Akt and lead to their degradation, 5 ?
Negative_regulation (inhibiting) of Hsp90
2) Confidence 0.30 Published 2010 Journal ASN NEURO Section Body Doc Link PMC2919983 Disease Relevance 0.17 Pain Relevance 0.08
In the present study, we provide the first evidence that a novel C-terminal Hsp90 inhibitor that increases Hsp70 expression is similarly effective in preventing death of unmyelinated neurons, demyelination of myelinated sensory neurons and was able to reverse pre-existing sensory deficits associated with the development of DPN in mice.
Negative_regulation (inhibitor) of Hsp90 in sensory neurons associated with demyelination, unmyelinated and death
3) Confidence 0.30 Published 2010 Journal ASN NEURO Section Body Doc Link PMC2919983 Disease Relevance 1.19 Pain Relevance 0.10
KU-32 is a novobiocin-based Hsp90 inhibitor containing an acetamide substitution on the coumarin ring (Figure 1A).
Negative_regulation (inhibitor) of Hsp90
4) Confidence 0.30 Published 2010 Journal ASN NEURO Section Body Doc Link PMC2919983 Disease Relevance 0.19 Pain Relevance 0.07
Inhibiting the chaperone activity of Hsp90 blocks protein folding and leads to client protein degradation (Powers and Workman, 2007).
Negative_regulation (Inhibiting) of Hsp90
5) Confidence 0.30 Published 2010 Journal ASN NEURO Section Body Doc Link PMC2919983 Disease Relevance 0.19 Pain Relevance 0
KU-32 (N-{7-[(2R,3R,4S,5R)-3,4-dihydroxy-5-methoxy-6,6-dimethyl-tetrahydro-2H-pyran-2-yloxy]-8-methyl-2-oxo-2H-chromen-3-yl}acetamide) was developed as a novel, novobiocin-based, C-terminal inhibitor of Hsp90 whose ability to increase Hsp70 expression is linked to the presence of an acetamide substitution of the prenylated benzamide moiety of novobiocin.
Negative_regulation (inhibitor) of Hsp90
6) Confidence 0.30 Published 2010 Journal ASN NEURO Section Abstract Doc Link PMC2919983 Disease Relevance 0.78 Pain Relevance 0.12
Our results provide compelling evidence that inhibiting Hsp90 can protect against sensory neuron death and demyelination and reverse the sensory deficits associated with DPN.
Negative_regulation (inhibiting) of Hsp90 in sensory neuron associated with demyelination and death
7) Confidence 0.30 Published 2010 Journal ASN NEURO Section Body Doc Link PMC2919983 Disease Relevance 0.34 Pain Relevance 0.13
Thus Hsp90 inhibitors can be useful as both chemotherapeutic and neuroprotective agents, and their primary biological outcome is dictated by the therapeutic window that dissociates client protein degradation and cytotoxicity from the cytoprotective induction of an HSR (Peterson and Blagg, 2009).
Negative_regulation (inhibitors) of Hsp90
8) Confidence 0.30 Published 2010 Journal ASN NEURO Section Body Doc Link PMC2919983 Disease Relevance 0.07 Pain Relevance 0
secretion was reduced in the presence of the HSP-90 inhibitor geldanamycin D (Fig. 1B).
Negative_regulation (inhibitor) of HSP-90
9) Confidence 0.07 Published 2009 Journal PLoS Pathogens Section Body Doc Link PMC2722371 Disease Relevance 0.05 Pain Relevance 0.08
Gedunin was recently shown to manifest anticancer activity via inhibition of the 90 kDa heat shock protein (Hsp90) folding machinery and to induce the degradation of Hsp90-dependent client proteins similar to other Hsp90 inhibitors.
Negative_regulation (inhibition) of 90 kDa heat shock protein associated with shock
10) Confidence 0.07 Published 2010 Journal PLoS ONE Section Body Doc Link PMC2903477 Disease Relevance 0.21 Pain Relevance 0.07

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