INT319611

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Context Info
Confidence 0.41
First Reported 2010
Last Reported 2010
Negated 0
Speculated 0
Reported most in Body
Documents 1
Total Number 3
Disease Relevance 0.87
Pain Relevance 0

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

plasma membrane (Nfe2l2) nucleus (Nfe2l2) DNA binding (Nfe2l2)
cytoplasm (Nfe2l2)
Nfe2l2 (Mus musculus)
Pain Link Frequency Relevance Heat
Paracetamol 3 5.00 Very Low Very Low Very Low
Disease Link Frequency Relevance Heat
Stress 69 97.84 Very High Very High Very High
Chronic Disease 3 58.32 Quite High
Targeted Disruption 9 50.08 Quite High
Death 3 24.64 Low Low
Cancer 18 10.24 Low Low
Sprains And Strains 3 5.00 Very Low Very Low Very Low
Aging 3 5.00 Very Low Very Low Very Low

Sentences Mentioned In

Key: Protein Mutation Event Anatomy Negation Speculation Pain term Disease term
Some of these findings were demonstrated in a model accounting for the degradation of the NRF2 transcription factor by CRIF1 and KEAP1 (see Fig. 9 and its legend).
Positive_regulation (accounting) of Protein_catabolism (degradation) of NRF2
1) Confidence 0.41 Published 2010 Journal The Journal of Biological Chemistry Section Body Doc Link PMC2898415 Disease Relevance 0.33 Pain Relevance 0
Both CRIF1 and KEAP1 1) function at the post-transcription level; 2) regulate NRF2 protein levels by binding the N-terminal region of NRF2; 3) promote ubiquitination of the same cluster of N-terminal NRF2 lysine residues; 4) promote proteasome-mediated degradation of NRF2; and 5) function under the reducing conditions normally present in cells.
Positive_regulation (mediated) of Protein_catabolism (degradation) of NRF2
2) Confidence 0.38 Published 2010 Journal The Journal of Biological Chemistry Section Body Doc Link PMC2898415 Disease Relevance 0.20 Pain Relevance 0
In addition, we found that CRIF1, unlike KEAP1 (which only interacts with N-terminal region of NRF2), physically interacts with both N- and C-terminal regions of NRF2 and promotes NRF2 ubiquitination and subsequent proteasome-mediated NRF2 protein degradation.



Positive_regulation (mediated) of Protein_catabolism (degradation) of NRF2
3) Confidence 0.38 Published 2010 Journal The Journal of Biological Chemistry Section Abstract Doc Link PMC2898415 Disease Relevance 0.34 Pain Relevance 0

General Comments

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