INT133898

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Context Info
Confidence 0.30
First Reported 2006
Last Reported 2010
Negated 2
Speculated 0
Reported most in Body
Documents 17
Total Number 18
Disease Relevance 8.83
Pain Relevance 1.12

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
BT-474 3
legs 1
HSP90AA1 (Homo sapiens)
Pain Link Frequency Relevance Heat
corticosteroid 6 100.00 Very High Very High Very High
Potency 33 98.90 Very High Very High Very High
abdominal pain 5 98.30 Very High Very High Very High
Pain 6 85.20 High High
Inflammation 30 84.84 Quite High
cINOD 1 82.80 Quite High
rheumatoid arthritis 11 76.44 Quite High
Inflammatory mediators 1 53.84 Quite High
headache 4 29.64 Quite Low
Arthritis 31 27.44 Quite Low
Disease Link Frequency Relevance Heat
Nephritis 7 100.00 Very High Very High Very High
Purpura 3 100.00 Very High Very High Very High
Pharyngitis 1 99.88 Very High Very High Very High
Cancer 684 99.84 Very High Very High Very High
Proteinuria 2 99.04 Very High Very High Very High
Stress 51 99.00 Very High Very High Very High
Abdominal Pain 5 98.30 Very High Very High Very High
Shock 134 93.28 High High
Breast Cancer 419 90.64 High High
Lymphatic System Cancer 31 88.00 High High

Sentences Mentioned In

Key: Protein Mutation Event Anatomy Negation Speculation Pain term Disease term
We report the case of a 25-year-old man with abdominal pain, purpura on the legs and proteinuria occurring 2 weeks after acute tonsillitis, and admitted to our hospital with suspected Henoch-Schönlein purpura nephritis (HSPN).
HSPN Binding (admitted) of in legs associated with pharyngitis, purpura, abdominal pain, nephritis and proteinuria
1) Confidence 0.30 Published 2006 Journal Clin. Nephrol. Section Abstract Doc Link 16509462 Disease Relevance 1.07 Pain Relevance 0.10
NVP-AUY922 appears to be more potent than 17-AAG at inhibiting the HSP90-p23 interaction.
HSP90-p23 Binding (interaction) of
2) Confidence 0.23 Published 2008 Journal Breast Cancer Res Section Body Doc Link PMC2397535 Disease Relevance 0.09 Pain Relevance 0.05
HSP90-p23 interaction requires ATP binding but not ATP hydrolysis in biochemical assays, and p23 specifically recognizes HSP90-ATP complexes but not HSP90 alone [28].
HSP90 Neg (not) Binding (complexes) of
3) Confidence 0.23 Published 2008 Journal Breast Cancer Res Section Body Doc Link PMC2397535 Disease Relevance 0.12 Pain Relevance 0
The biodistribution and pharmacokinetic profile of NVP-AUY922 in the BT-474 xenograft model encouraged us to assess whether NVP-AUY922 is capable of directly interfering with the catalytic cycle of HSP90 with concomitant depletion of HSP90 client proteins in vivo (Figure 2b).
HSP90 Binding (interfering) of in BT-474
4) Confidence 0.23 Published 2008 Journal Breast Cancer Res Section Body Doc Link PMC2397535 Disease Relevance 0.23 Pain Relevance 0
To asses whether systemic administration of NVP-AUY922 could affect the association between p23 and HSP90 observed in vitro, HSP90?
HSP90 Binding (association) of
5) Confidence 0.23 Published 2008 Journal Breast Cancer Res Section Body Doc Link PMC2397535 Disease Relevance 0.21 Pain Relevance 0
NVP-AUY922 binds very potently to HSP90 in a competitive biochemical assay [23,26].
HSP90 Binding (binds) of
6) Confidence 0.23 Published 2008 Journal Breast Cancer Res Section Body Doc Link PMC2397535 Disease Relevance 0.51 Pain Relevance 0.05
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).
HSP90-p23 Binding (interaction) of associated with cancer
7) Confidence 0.23 Published 2008 Journal Breast Cancer Res Section Body Doc Link PMC2397535 Disease Relevance 0.10 Pain Relevance 0.03
The high biochemical potency correlated with the ability of NVP-AUY922 to directly interfere with the HSP90-p23 complex both in BT-474 cells grown in culture and as xenografts.
HSP90-p23 Binding (interfere) of in BT-474 associated with potency
8) Confidence 0.23 Published 2008 Journal Breast Cancer Res Section Body Doc Link PMC2397535 Disease Relevance 0.52 Pain Relevance 0.05
The biodistribution and pharmacokinetic profile of NVP-AUY922 in the BT-474 xenograft model encouraged us to assess whether NVP-AUY922 is capable of directly interfering with the catalytic cycle of HSP90 with concomitant depletion of HSP90 client proteins in vivo (Figure 2b).
HSP90 Binding (interfering) of in BT-474
9) Confidence 0.23 Published 2008 Journal Breast Cancer Res Section Body Doc Link PMC2397535 Disease Relevance 0.23 Pain Relevance 0
HSP90-p23 interaction requires ATP binding but not ATP hydrolysis in biochemical assays, and p23 specifically recognizes HSP90-ATP complexes but not HSP90 alone [28].
HSP90 Neg (not) Binding (complexes) of
10) Confidence 0.23 Published 2008 Journal Breast Cancer Res Section Body Doc Link PMC2397535 Disease Relevance 0.12 Pain Relevance 0
HSP90-p23 interaction requires ATP binding but not ATP hydrolysis in biochemical assays, and p23 specifically recognizes HSP90-ATP complexes but not HSP90 alone [28].
HSP90-p23 Binding (interaction) of
11) Confidence 0.23 Published 2008 Journal Breast Cancer Res Section Body Doc Link PMC2397535 Disease Relevance 0.17 Pain Relevance 0
A fundamental step in the activation of HSF1 is nuclear translocation.24,25 In the absence of stress, HSF1 is retained in the cytoplasm by inhibitory associations with Hsp70, Hsp90, and various cochaperones.(26) We demonstrated that HNE promotes the nuclear translocation of HSF1 using Western blot analysis, and showed the enhanced transcription of a luciferase reporter gene under the regulation of a conserved heat shock element.(27)
Hsp90 Binding (associations) of associated with stress and shock
12) Confidence 0.21 Published 2010 Journal Accounts of Chemical Research Section Body Doc Link PMC2873822 Disease Relevance 0.92 Pain Relevance 0
HNE treatment has been shown in vitro to adduct specific amino acid residues on both Hsp70 and Hsp90, which correlates with their reduced ability to bind and properly fold client proteins.28,29 We performed coimmunoprecipitation experiments with myc-tagged Hsp70, demonstrating that its association with HSF1 is disrupted by HNE treatment.
Hsp90 Binding (bind) of
13) Confidence 0.21 Published 2010 Journal Accounts of Chemical Research Section Body Doc Link PMC2873822 Disease Relevance 0.75 Pain Relevance 0
Tanespimycin (17-AAG) is an ansamycin antibiotic that binds to Hsp90 and induces the degradation of proteins that require this chaperone thereby inducing tumor cell regression.
Hsp90 Binding (binds) of associated with cancer
14) Confidence 0.13 Published 2008 Journal J Hematol Oncol Section Body Doc Link PMC2579406 Disease Relevance 1.19 Pain Relevance 0.08
The cGCR is a multiprotein complex that sheds HSP90 and other chaperones after GC binding, followed by nuclear translocation of the complex.
HSP90 Binding (binding) of associated with corticosteroid
15) Confidence 0.12 Published 2008 Journal International Journal of Nanomedicine Section Body Doc Link PMC2626937 Disease Relevance 1.06 Pain Relevance 0.77
Furthermore, a number of cytoplasmic proteins, including tubulin and HSP90, have now been shown to be acetylated by HDAC [69-73]
HSP90 Binding (number) of
16) Confidence 0.07 Published 2010 Journal J Hematol Oncol Section Body Doc Link PMC2827364 Disease Relevance 0.57 Pain Relevance 0
Furthermore, a number of cytoplasmic proteins, including tubulin and HSP90, have now been shown to be acetylated by HDAC [69-73]
HSP90 Binding (tubulin) of
17) Confidence 0.07 Published 2010 Journal J Hematol Oncol Section Body Doc Link PMC2827364 Disease Relevance 0.57 Pain Relevance 0
Akt is a substrate of the chaperone Hsp90. 17AAG downregulated Akt by virtue of its inhibitory role on Hsp90.
Hsp90 Binding (role) of
18) Confidence 0.05 Published 2010 Journal PLoS ONE Section Body Doc Link PMC2806839 Disease Relevance 0.37 Pain Relevance 0

General Comments

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