INT320784

From wiki-pain
Jump to: navigation, search
Context Info
Confidence 0.61
First Reported 2010
Last Reported 2010
Negated 0
Speculated 0
Reported most in Body
Documents 3
Total Number 4
Disease Relevance 2.41
Pain Relevance 0.34

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) protein binding transcription factor activity (Hif1a) DNA binding (Hif1a)
Hif1a (Mus musculus)
Pain Link Frequency Relevance Heat
imagery 225 92.36 High High
cytokine 4 82.08 Quite High
Kinase C 1 40.48 Quite Low
ischemia 5 23.92 Low Low
positron emission tomography 7 5.00 Very Low Very Low Very Low
Inflammation 6 5.00 Very Low Very Low Very Low
anesthesia 3 5.00 Very Low Very Low Very Low
antagonist 3 5.00 Very Low Very Low Very Low
metalloproteinase 3 5.00 Very Low Very Low Very Low
withdrawal 2 5.00 Very Low Very Low Very Low
Disease Link Frequency Relevance Heat
Hypoxia 38 97.60 Very High Very High Very High
Cancer 234 97.52 Very High Very High Very High
Targeted Disruption 47 81.64 Quite High
Peripheral Arterial Disease 4 59.04 Quite High
Metastasis 9 58.24 Quite High
Injury 16 53.48 Quite High
Disease 4 40.72 Quite Low
Hematological Disease 2 34.76 Quite Low
Cv Unclassified Under Development 13 23.92 Low Low
Von Hippel-lindau Syndrome 1 5.28 Low Low

Sentences Mentioned In

Key: Protein Mutation Event Anatomy Negation Speculation Pain term Disease term
/pVHL interaction [8] and the subsequent ubiquitinylation and degradation of HIF-1?
Protein_catabolism (degradation) of HIF-1
1) Confidence 0.61 Published 2010 Journal PLoS ONE Section Body Doc Link PMC2908132 Disease Relevance 0.27 Pain Relevance 0
In short, HIF-1 has an oxygen dependent degradation domain (ODD) which is hydroxylated in an oxygen dependent manner by prolyl hydroxylases.
Protein_catabolism (degradation) of HIF-1
2) Confidence 0.44 Published 2010 Journal Angiogenesis Section Body Doc Link PMC2911541 Disease Relevance 0.84 Pain Relevance 0.14
As a result, the ODD binds the Von Hippel-Lindau factor (VHL) under normoxic conditions, targeting HIF-1 for proteasomal degradation.
Protein_catabolism (degradation) of HIF-1
3) Confidence 0.29 Published 2010 Journal Angiogenesis Section Body Doc Link PMC2911541 Disease Relevance 0.68 Pain Relevance 0.12
Normoxic conditions favor ubiquitin-dependent proteosome-mediated degradation of HIF-1?
Protein_catabolism (degradation) of HIF-1
4) Confidence 0.27 Published 2010 Journal Journal of Oncology Section Body Doc Link PMC2902148 Disease Relevance 0.62 Pain Relevance 0.08

General Comments

This test has worked.

Personal tools
Namespaces

Variants
Actions
Navigation
Toolbox