INT100378

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Context Info
Confidence 0.96
First Reported 2001
Last Reported 2010
Negated 0
Speculated 0
Reported most in Body
Documents 7
Total Number 7
Disease Relevance 5.05
Pain Relevance 0.80

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 (HIF1A) signal transduction (HIF1A) nucleolus (HIF1A)
nucleus (HIF1A) transcription factor binding (HIF1A) cytoplasm (HIF1A)
Anatomy Link Frequency
endothelial cells 1
HIF1A (Homo sapiens)
Pain Link Frequency Relevance Heat
cINOD 9 98.64 Very High Very High Very High
Central nervous system 3 96.48 Very High Very High Very High
antagonist 30 87.04 High High
Inflammation 49 76.88 Quite High
metalloproteinase 14 76.76 Quite High
agonist 44 70.80 Quite High
Dopamine 1 70.48 Quite High
Inflammatory response 3 61.44 Quite High
palliative 1 40.88 Quite Low
rheumatoid arthritis 68 26.00 Quite Low
Disease Link Frequency Relevance Heat
Hypoxia 138 100.00 Very High Very High Very High
Cancer 355 99.40 Very High Very High Very High
Brain Tumor 3 97.16 Very High Very High Very High
Ovarian Cancer 23 97.04 Very High Very High Very High
Carcinoma 4 93.56 High High
Death 11 91.92 High High
Apoptosis 61 90.32 High High
Necrosis 5 86.24 High High
INFLAMMATION 48 76.88 Quite High
Hemangioma 1 70.28 Quite High

Sentences Mentioned In

Key: Protein Mutation Event Anatomy Negation Speculation Pain term Disease term
Taken together, these results indicate that NSAIDs inhibit hypoxia-induced angiogenesis in endothelial cells by inhibiting VEGF and Flt-1 expression through increased VHL expression and the resulting ubiquitination and degradation of HIF-1alpha.
Protein_catabolism (degradation) of HIF-1alpha in endothelial cells associated with hypoxia and cinod
1) Confidence 0.96 Published 2002 Journal FASEB J. Section Abstract Doc Link 11772947 Disease Relevance 0.81 Pain Relevance 0.51
levels are reduced by constant proteosomal degradation, whereas under hypoxic conditions the HIF-1?
Protein_catabolism (degradation) of HIF associated with hypoxia
2) Confidence 0.64 Published 2010 Journal Acta Histochemica et Cytochemica Section Body Doc Link PMC2875861 Disease Relevance 0.66 Pain Relevance 0.11
The alpha-subunit of HIF-1 is rapidly degraded by the proteasome under normoxic conditions, but it is stabilized on occurrence of hypoxia.
Protein_catabolism (degraded) of HIF-1 associated with hypoxia
3) Confidence 0.52 Published 2001 Journal Adv. Exp. Med. Biol. Section Abstract Doc Link 11950137 Disease Relevance 0.77 Pain Relevance 0.04
The VHL protein contains a binding site in the oxygen-dependent degradation domain (ODD) of HIF-1?
Protein_catabolism (degradation) of HIF-1
4) Confidence 0.52 Published 2003 Journal Mol Cancer Section Body Doc Link PMC150383 Disease Relevance 0.58 Pain Relevance 0.05
for the tumor suppressor protein von Hippel-Lindau (pVHL) E3 ligase complex, which mediates ubiquitination and proteasomal degradation of HIF-1?
Protein_catabolism (degradation) of HIF-1 associated with cancer
5) Confidence 0.29 Published 2010 Journal PPAR Research Section Body Doc Link PMC2829627 Disease Relevance 0.86 Pain Relevance 0.03
Degradation of HIF-1?
Protein_catabolism (Degradation) of HIF-1
6) Confidence 0.11 Published 2004 Journal J Transl Med Section Body Doc Link PMC436068 Disease Relevance 0.90 Pain Relevance 0.07
It should be noted that the degradation of HIF-1?
Protein_catabolism (degradation) of HIF-1
7) Confidence 0.06 Published 2004 Journal Arthritis Res Ther Section Body Doc Link PMC1064874 Disease Relevance 0.46 Pain Relevance 0

General Comments

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