INT341195

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Context Info
Confidence 0.38
First Reported 2010
Last Reported 2010
Negated 0
Speculated 0
Reported most in Body
Documents 1
Total Number 19
Disease Relevance 3.87
Pain Relevance 0.92

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

RNA binding (Eif4e) translation (Eif4e) protein complex (Eif4e)
cytoplasm (Eif4e)
Anatomy Link Frequency
cerebral cortex 1
Eif4e (Mus musculus)
Pain Link Frequency Relevance Heat
ischemia 684 96.86 Very High Very High Very High
cerebral cortex 190 96.76 Very High Very High Very High
alcohol 19 69.20 Quite High
addiction 19 5.00 Very Low Very Low Very Low
anesthesia 19 5.00 Very Low Very Low Very Low
Disease Link Frequency Relevance Heat
Stress 532 97.24 Very High Very High Very High
Cv Unclassified Under Development 665 96.86 Very High Very High Very High
Repression 19 88.16 High High
Cv General 4 Under Development 19 71.88 Quite High
Glioma 19 70.64 Quite High
Alzheimer's Dementia 19 70.32 Quite High
Toxicity 19 69.56 Quite High
Brain Disease 19 68.16 Quite High
Hypoxia 114 30.32 Quite Low
Cancer 114 5.00 Very Low Very Low Very Low

Sentences Mentioned In

Key: Protein Mutation Event Anatomy Negation Speculation Pain term Disease term
However, their individual contribution to the control of eIF4E binding is controversial (6).
eIF4E Binding (binding) of
1) Confidence 0.38 Published 2010 Journal The Journal of Biological Chemistry Section Body Doc Link PMC2966049 Disease Relevance 0 Pain Relevance 0
Conversely, (hyper)phosphorylation of 4E-BPs reduces their affinity for eIF4E and releases them from eIF4E.
eIF4E Binding (affinity) of
2) Confidence 0.38 Published 2010 Journal The Journal of Biological Chemistry Section Body Doc Link PMC2966049 Disease Relevance 0 Pain Relevance 0
Phosphorylation at Ser64 and Thr69 seems to regulate binding to eIF4E, but these phosphorylation reactions alone are insufficient to block binding to eIF4E, which indicates that combination with Thr36/Thr45 phosphorylation is necessary to dissociate 4E-BP1 from eIF4E (6, 10, 36).
eIF4E Binding (binding) of
3) Confidence 0.29 Published 2010 Journal The Journal of Biological Chemistry Section Body Doc Link PMC2966049 Disease Relevance 0.47 Pain Relevance 0.06
Active hypophosphorylated forms of 4E-BPs bind to eIF4E, compete with eIF4G, and inhibit eIF4G binding to eIF4E, which prevents eIF4F complex formation and inhibits cap-dependent translation (1–8).
eIF4E Binding (binding) of
4) Confidence 0.29 Published 2010 Journal The Journal of Biological Chemistry Section Body Doc Link PMC2966049 Disease Relevance 0 Pain Relevance 0
Phosphorylation of Thr36/Thr45 does not regulate the binding of 4E-BP1 to eIF4E directly (6), whereas phosphorylation at Ser64 and Thr69 is insufficient to prevent binding to eIF4E (10).
eIF4E Binding (binding) of
5) Confidence 0.29 Published 2010 Journal The Journal of Biological Chemistry Section Body Doc Link PMC2966049 Disease Relevance 0 Pain Relevance 0
The R3d group had a significant amount of 4E-BP1 phosphorylated at Thr69/Thr36/Thr45, and neither was associated with eIF4E; therefore, we share the hypothesis that Ser64 phosphorylation is dispensable for dissociation from eIF4E.
eIF4E Binding (associated) of
6) Confidence 0.29 Published 2010 Journal The Journal of Biological Chemistry Section Body Doc Link PMC2966049 Disease Relevance 0.09 Pain Relevance 0
Phosphorylation at Ser64 and Thr69 seems to regulate binding to eIF4E, but these phosphorylation reactions alone are insufficient to block binding to eIF4E, which indicates that combination with Thr36/Thr45 phosphorylation is necessary to dissociate 4E-BP1 from eIF4E (6, 10, 36).
eIF4E Binding (binding) of
7) Confidence 0.29 Published 2010 Journal The Journal of Biological Chemistry Section Body Doc Link PMC2966049 Disease Relevance 0.45 Pain Relevance 0.06
Our results demonstrate that Thr69 phosphorylation alone allows binding to eIF4E, and subsequent Thr36/Thr45 phosphorylation is sufficient to dissociate 4E-BP1 from eIF4E.
eIF4E Binding (binding) of
8) Confidence 0.29 Published 2010 Journal The Journal of Biological Chemistry Section Body Doc Link PMC2966049 Disease Relevance 0.13 Pain Relevance 0
The individual contribution of the 4E-BP1 phosphorylation sites to the control of eIF4E binding remains controversial. 4E-BP1 phosphorylated on Th36/Thr45 retains the ability to interact with eIF4E (10).
eIF4E Binding (binding) of
9) Confidence 0.29 Published 2010 Journal The Journal of Biological Chemistry Section Body Doc Link PMC2966049 Disease Relevance 0.52 Pain Relevance 0.07
However, Ser64 phosphorylation might be dispensable for dissociation from eIF4E (29), and it has suggested that phosphorylation at this site prevents the reassociation of eIF4E and 4E-BP1 (37).
eIF4E Binding (reassociation) of
10) Confidence 0.29 Published 2010 Journal The Journal of Biological Chemistry Section Body Doc Link PMC2966049 Disease Relevance 0.18 Pain Relevance 0
Active hypophosphorylated forms of 4E-BPs bind to eIF4E, compete with eIF4G, and inhibit eIF4G binding to eIF4E, which prevents eIF4F complex formation and inhibits cap-dependent translation (1–8).
eIF4E Binding (bind) of
11) Confidence 0.28 Published 2010 Journal The Journal of Biological Chemistry Section Body Doc Link PMC2966049 Disease Relevance 0 Pain Relevance 0
Thr69 phosphorylation alone allows binding to eIF4E, and subsequent Thr36/Thr45 phosphorylation was sufficient to dissociate 4E-BP1 from eIF4E, which led to eIF4E-4G interaction.
eIF4E Binding (binding) of
12) Confidence 0.28 Published 2010 Journal The Journal of Biological Chemistry Section Abstract Doc Link PMC2966049 Disease Relevance 0.38 Pain Relevance 0.06
forms were the forms bound to eIF4E, whereas the ?
eIF4E Binding (bound) of
13) Confidence 0.28 Published 2010 Journal The Journal of Biological Chemistry Section Body Doc Link PMC2966049 Disease Relevance 0.17 Pain Relevance 0.11
Two-dimensional gel electrophoresis and Western blotting of 4E-BP1 bound to eIF4E detected the ?
eIF4E Binding (bound) of
14) Confidence 0.28 Published 2010 Journal The Journal of Biological Chemistry Section Body Doc Link PMC2966049 Disease Relevance 0.14 Pain Relevance 0.16
form of 4E-BP1 were specific forms bound to eIF4E.
eIF4E Binding (bound) of
15) Confidence 0.28 Published 2010 Journal The Journal of Biological Chemistry Section Body Doc Link PMC2966049 Disease Relevance 0.29 Pain Relevance 0.12
A key step in this process is the assembly of eukaryotic initiation factor (eIF) 4F complex, which contains: the initiation factor eIF4A, an ATP-dependent RNA helicase; eIF4E, which binds to the mRNA 5?
eIF4E Binding (binds) of
16) Confidence 0.28 Published 2010 Journal The Journal of Biological Chemistry Section Body Doc Link PMC2966049 Disease Relevance 0 Pain Relevance 0
New Hierarchical Phosphorylation Pathway of the Translational Repressor eIF4E-binding Protein 1 (4E-BP1) in Ischemia-Reperfusion Stress*

Eukaryotic initiation factor (eIF) 4E-binding protein 1 (4E-BP1) is a translational repressor that is characterized by its capacity to bind specifically to eIF4E and inhibit its interaction with eIF4G.

eIF4E Binding (bind) of associated with stress and ischemia
17) Confidence 0.28 Published 2010 Journal The Journal of Biological Chemistry Section Title Doc Link PMC2966049 Disease Relevance 0.70 Pain Relevance 0.09
No significant changes in 4E-BP1 and eIF4G/eIF4E association were found in the R3d group when compared with the SHC3d control or between the cerebral cortex and hippocampal CA1 region (supplemental Fig.
eIF4E Binding (association) of in cerebral cortex associated with cerebral cortex
18) Confidence 0.28 Published 2010 Journal The Journal of Biological Chemistry Section Body Doc Link PMC2966049 Disease Relevance 0.19 Pain Relevance 0.17
In contrast, other studies have shown that Thr69 phosphorylation is crucial for dissociation from eIF4E (23, 37, 38).
eIF4E Binding (dissociation) of
19) Confidence 0.25 Published 2010 Journal The Journal of Biological Chemistry Section Body Doc Link PMC2966049 Disease Relevance 0.18 Pain Relevance 0

General Comments

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