INT166024

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Context Info
Confidence 0.46
First Reported 2008
Last Reported 2010
Negated 0
Speculated 0
Reported most in Body
Documents 5
Total Number 6
Disease Relevance 2.60
Pain Relevance 0.64

This is a graph with borders and nodes. Maybe there is an Imagemap used so the nodes may be linking to some Pages.

cell differentiation (AKT1) nucleoplasm (AKT1) transport (AKT1)
small molecule metabolic process (AKT1) enzyme binding (AKT1) carbohydrate metabolic process (AKT1)
AKT1 (Homo sapiens)
Pain Link Frequency Relevance Heat
aspirin 15 97.60 Very High Very High Very High
Bioavailability 7 67.96 Quite High
COX-2 inhibitor 25 59.96 Quite High
cINOD 6 58.12 Quite High
cva 2 51.16 Quite High
Inflammation 42 50.00 Quite Low
metalloproteinase 102 5.00 Very Low Very Low Very Low
cytokine 78 5.00 Very Low Very Low Very Low
chemokine 20 5.00 Very Low Very Low Very Low
Potency 11 5.00 Very Low Very Low Very Low
Disease Link Frequency Relevance Heat
Leukemia 19 99.60 Very High Very High Very High
Shock 9 98.64 Very High Very High Very High
Apoptosis 27 97.96 Very High Very High Very High
Cancer 149 85.84 High High
Herpes Simplex Virus 238 85.28 High High
Breast Cancer 36 78.68 Quite High
Lymphatic System Cancer 4 76.16 Quite High
Squamous Cell Carcinoma 3 75.00 Quite High
Adhesions 42 65.24 Quite High
Fibrosarcoma 17 62.44 Quite High

Sentences Mentioned In

Key: Protein Mutation Event Anatomy Negation Speculation Pain term Disease term
These findings collectively suggest that aspirin induces apoptosis in YD-8 cells and the induction may be correlated to activation of caspases, caspase-dependent Mcl-1 proteolysis, inactivation of ERK-1/2 and AKT, and activation of NF-kappaB.
Protein_catabolism (proteolysis) of AKT associated with aspirin and apoptosis
1) Confidence 0.46 Published 2010 Journal Toxicol In Vitro Section Abstract Doc Link 20116423 Disease Relevance 0.59 Pain Relevance 0.56
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 AKT
2) Confidence 0.39 Published 2008 Journal Breast Cancer Res Section Body Doc Link PMC2397535 Disease Relevance 0.41 Pain Relevance 0
As shown in Fig. 5C, PO at 12.5 µg/ml led to the decreased expression of PI3K and phosphorylation of its downstream target AKT.
Protein_catabolism (its) of AKT
3) Confidence 0.22 Published 2010 Journal PLoS ONE Section Body Doc Link PMC2925949 Disease Relevance 0.36 Pain Relevance 0.03
As shown in Fig. 5C, PO at 12.5 µg/ml led to the decreased expression of PI3K and phosphorylation of its downstream target AKT.
Protein_catabolism (downstream) of AKT
4) Confidence 0.22 Published 2010 Journal PLoS ONE Section Body Doc Link PMC2925949 Disease Relevance 0.36 Pain Relevance 0.03
They have been extensively studied for their ability to induce acetylation and to inhibit the ATP binding and chaperone function of heat shock protein (HSP) 90, promoting the polyubiquitylation and proteasomal degradation of the pro-growth and prosurvival client proteins Bcr-Abl, mutant FLT-3, c-Raf, and AKT in human leukemia cells [123].
Protein_catabolism (degradation) of AKT associated with leukemia and shock
5) Confidence 0.13 Published 2008 Journal Current Medicinal Chemistry Section Body Doc Link PMC2764862 Disease Relevance 0.68 Pain Relevance 0.03
The degree of RhoA or Rac-1 activation is determined by comparing readings from lysates prepared from various treatments.


Protein_catabolism (degree) of Rac
6) Confidence 0.05 Published 2010 Journal PLoS Pathogens Section Body Doc Link PMC2820536 Disease Relevance 0.21 Pain Relevance 0

General Comments

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