INT319682

From wiki-pain
Jump to: navigation, search
Context Info
Confidence 0.43
First Reported 2010
Last Reported 2010
Negated 0
Speculated 0
Reported most in Body
Documents 1
Total Number 20
Disease Relevance 1.41
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.

nucleus (Nfe2l2, Gadd45gip1) mitochondrion (Gadd45gip1) plasma membrane (Nfe2l2)
cell cycle (Gadd45gip1) DNA binding (Nfe2l2) cytoplasm (Nfe2l2)
Nfe2l2 (Mus musculus)
Gadd45gip1 (Mus musculus)
Pain Link Frequency Relevance Heat
Paracetamol 20 5.00 Very Low Very Low Very Low
Disease Link Frequency Relevance Heat
Stress 460 99.32 Very High Very High Very High
Targeted Disruption 60 10.00 Low Low
Cancer 120 5.00 Very Low Very Low Very Low
Sprains And Strains 20 5.00 Very Low Very Low Very Low
Aging 20 5.00 Very Low Very Low Very Low
Chronic Disease 20 5.00 Very Low Very Low Very Low
Death 20 5.00 Very Low Very Low Very Low

Sentences Mentioned In

Key: Protein Mutation Event Anatomy Negation Speculation Pain term Disease term
This experiment showed that endogenous CRIF1, like exogenous CRIF1, can interact with NRF2 in the absence or presence of either of two NRF2-inducing agents (Fig. 1, C and D), indicating that the CRIF1-NRF2 interaction is redox-independent.
NRF2 Binding (interact) of CRIF1
1) Confidence 0.43 Published 2010 Journal The Journal of Biological Chemistry Section Body Doc Link PMC2898415 Disease Relevance 0.17 Pain Relevance 0
There are also several differences between the activity of CRIF1 and KEAP1; for example, 1) CRIF1 interacts with both the N and C termini of NRF2 protein, whereas KEAP1 interacts with only the N terminus of NRF2; and 2) KEAP1 cannot interact with ETGE point mutants of NRF2, whereas CRIF1 can.
NRF2 Binding (interacts) of CRIF1
2) Confidence 0.43 Published 2010 Journal The Journal of Biological Chemistry Section Body Doc Link PMC2898415 Disease Relevance 0.20 Pain Relevance 0
To confirm this result and to test for a direct NRF2-CRIF1 protein-protein interaction, we performed reciprocal co-immunoprecipitation experiments with total lysates prepared from cells transfected with expression vectors for FLAG-NRF2, GFP-CRIF1, both, or neither.
NRF2 Binding (interaction) of CRIF1 protein
3) Confidence 0.43 Published 2010 Journal The Journal of Biological Chemistry Section Body Doc Link PMC2898415 Disease Relevance 0.05 Pain Relevance 0
Both slower and faster migrating forms of CRIF1 IVT seem to interact with NRF2 not only in vitro but also in vivo (Fig. 1, C and D).
NRF2 Binding (interact) of CRIF1 IVT
4) Confidence 0.43 Published 2010 Journal The Journal of Biological Chemistry Section Body Doc Link PMC2898415 Disease Relevance 0 Pain Relevance 0
Next, we identified which regions of NRF2 interact with CRIF1.
NRF2 Binding (interact) of CRIF1
5) Confidence 0.43 Published 2010 Journal The Journal of Biological Chemistry Section Body Doc Link PMC2898415 Disease Relevance 0 Pain Relevance 0
These results specify that CRIF1 partially interacts with the bZIP domain (aa 435–563) of NRF2.


NRF2 Binding (interacts) of CRIF1
6) Confidence 0.43 Published 2010 Journal The Journal of Biological Chemistry Section Body Doc Link PMC2898415 Disease Relevance 0 Pain Relevance 0
This experiment showed that endogenous CRIF1, like exogenous CRIF1, can interact with NRF2 in the absence or presence of either of two NRF2-inducing agents (Fig. 1, C and D), indicating that the CRIF1-NRF2 interaction is redox-independent.
NRF2 Binding (interact) of CRIF1
7) Confidence 0.43 Published 2010 Journal The Journal of Biological Chemistry Section Body Doc Link PMC2898415 Disease Relevance 0.17 Pain Relevance 0
To test whether endogenous CRIF1 can also bind NRF2 under oxidative stress conditions, cells transfected with GFP-NRF2 for 24 h were treated with either t-BHQ or SFN, another NRF2-inducing agent, and then used for IP-WB analysis with an anti-GFP antibody (Fig. 1, C and D).
NRF2 Binding (bind) of CRIF1 associated with stress
8) Confidence 0.43 Published 2010 Journal The Journal of Biological Chemistry Section Body Doc Link PMC2898415 Disease Relevance 0.19 Pain Relevance 0
Next, we asked whether the functional interactions observed between exogenous CRIF1 and NRF2 proteins reflect similar functional interaction between endogenous CRIF1 and NRF2 proteins.
NRF2 Binding (interaction) of CRIF1
9) Confidence 0.33 Published 2010 Journal The Journal of Biological Chemistry Section Body Doc Link PMC2898415 Disease Relevance 0 Pain Relevance 0
Next, we asked whether the functional interactions observed between exogenous CRIF1 and NRF2 proteins reflect similar functional interaction between endogenous CRIF1 and NRF2 proteins.
NRF2 Binding (interaction) of CRIF1
10) Confidence 0.33 Published 2010 Journal The Journal of Biological Chemistry Section Body Doc Link PMC2898415 Disease Relevance 0 Pain Relevance 0
Because CRIF1 can bind the N- and C-terminal region of NRF2 (Fig. 2C), we tested whether CRIF1 can also drive ubiquitination at the C terminus of NRF2.
NRF2 Binding (bind) of CRIF1
11) Confidence 0.33 Published 2010 Journal The Journal of Biological Chemistry Section Body Doc Link PMC2898415 Disease Relevance 0 Pain Relevance 0
There are also several differences between the activity of CRIF1 and KEAP1; for example, 1) CRIF1 interacts with both the N and C termini of NRF2 protein, whereas KEAP1 interacts with only the N terminus of NRF2; and 2) KEAP1 cannot interact with ETGE point mutants of NRF2, whereas CRIF1 can.
NRF2 Binding (interacts) of CRIF1
12) Confidence 0.33 Published 2010 Journal The Journal of Biological Chemistry Section Body Doc Link PMC2898415 Disease Relevance 0.21 Pain Relevance 0
We quantified the amount of CRIF1 (slower migrating form) interacting with immunoprecipitated GFP-NRF2 and found that t-BHQ or SFN does not significantly change the amount of CRIF1 interacting with NRF2.
NRF2 Binding (interacting) of CRIF1
13) Confidence 0.32 Published 2010 Journal The Journal of Biological Chemistry Section Body Doc Link PMC2898415 Disease Relevance 0.13 Pain Relevance 0
These results strongly suggest that CRIF1 can directly interact with NRF2 in vitro.
NRF2 Binding (interact) of CRIF1
14) Confidence 0.32 Published 2010 Journal The Journal of Biological Chemistry Section Body Doc Link PMC2898415 Disease Relevance 0 Pain Relevance 0
Because CRIF1 and NRF2 interact, we tested whether CRIF1 can affect NRF2 protein levels under normal reducing conditions.
NRF2 Binding (interact) of CRIF1
15) Confidence 0.32 Published 2010 Journal The Journal of Biological Chemistry Section Body Doc Link PMC2898415 Disease Relevance 0 Pain Relevance 0
When mixtures of unlabeled IVT-FLAG-CRIF1 and each of the 35S-labeled NRF2 deletion mutants were immunoprecipitated with the anti-FLAG antibody, we found that CRIF1 co-immunoprecipitated with both the most N-terminal (aa 1–100) and the most C-terminal (aa 435–605) regions of NRF2 (Fig. 2C), indicating that NRF2 contains at least two domains capable of binding CRIF1.
NRF2 Binding (binding) of CRIF1
16) Confidence 0.32 Published 2010 Journal The Journal of Biological Chemistry Section Body Doc Link PMC2898415 Disease Relevance 0 Pain Relevance 0
We only observed the decrease of CRIF1 interaction with NRF2 8 h following t-BHQ treatment.
NRF2 Binding (interaction) of CRIF1
17) Confidence 0.32 Published 2010 Journal The Journal of Biological Chemistry Section Body Doc Link PMC2898415 Disease Relevance 0.11 Pain Relevance 0
We quantified the amount of CRIF1 (slower migrating form) interacting with immunoprecipitated GFP-NRF2 and found that t-BHQ or SFN does not significantly change the amount of CRIF1 interacting with NRF2.
NRF2 Binding (interacting) of CRIF1
18) Confidence 0.32 Published 2010 Journal The Journal of Biological Chemistry Section Body Doc Link PMC2898415 Disease Relevance 0.12 Pain Relevance 0
To confirm this result and to test for a direct NRF2-CRIF1 protein-protein interaction, we performed reciprocal co-immunoprecipitation experiments with total lysates prepared from cells transfected with expression vectors for FLAG-NRF2, GFP-CRIF1, both, or neither.
NRF2 Binding (interaction) of CRIF1 protein
19) Confidence 0.32 Published 2010 Journal The Journal of Biological Chemistry Section Body Doc Link PMC2898415 Disease Relevance 0.05 Pain Relevance 0
Next, we asked whether the functional interactions observed between exogenous CRIF1 and NRF2 proteins reflect similar functional interaction between endogenous CRIF1 and NRF2 proteins.
NRF2 Binding (interaction) of CRIF1
20) Confidence 0.32 Published 2010 Journal The Journal of Biological Chemistry Section Body Doc Link PMC2898415 Disease Relevance 0 Pain Relevance 0

General Comments

This test has worked.

Personal tools
Namespaces

Variants
Actions
Navigation
Toolbox