INT44888

From wiki-pain
Jump to: navigation, search
Context Info
Confidence 0.80
First Reported 1983
Last Reported 2010
Negated 1
Speculated 0
Reported most in Abstract
Documents 12
Total Number 12
Disease Relevance 5.70
Pain Relevance 1.70

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

cytosol (EIF2S1) RNA binding (EIF2S1) nucleus (EIF2S1)
translation (EIF2S1) cytoplasm (EIF2S1)
Anatomy Link Frequency
reticulocyte 1
reticulum 1
EIF2S1 (Homo sapiens)
Pain Link Frequency Relevance Heat
Pain 7 99.32 Very High Very High Very High
Paracetamol 8 99.28 Very High Very High Very High
cINOD 8 84.84 Quite High
Inflammation 4 84.36 Quite High
ischemia 2 80.36 Quite High
lidocaine 1 5.00 Very Low Very Low Very Low
anesthesia 1 5.00 Very Low Very Low Very Low
Disease Link Frequency Relevance Heat
Stress 34 99.82 Very High Very High Very High
Pain 7 99.32 Very High Very High Very High
Apoptosis 11 98.36 Very High Very High Very High
Injury 2 94.16 High High
Hypoxia 31 92.80 High High
Ehrlich Tumor Carcinoma 7 87.08 High High
INFLAMMATION 4 84.36 Quite High
Cv General 4 Under Development 2 80.36 Quite High
Disease 8 79.44 Quite High
Death 2 77.36 Quite High

Sentences Mentioned In

Key: Protein Mutation Event Anatomy Negation Speculation Pain term Disease term
Phosphorylation of eukaryotic translation initiation factor 2 alpha (eIF2alpha) is a critical convergence point of the integrated stress response (ISR), which supports eukaryotic cellular adaptation to diverse stressful conditions, including the endoplasmic reticulum (ER) stress by global protein translational arrest and induction of numerous stress-triggered cytoprotective genes.
Phosphorylation (Phosphorylation) of eIF2alpha in reticulum associated with stress
1) Confidence 0.80 Published 2010 Journal Carcinogenesis Section Abstract Doc Link 20130018 Disease Relevance 0.75 Pain Relevance 0.30
ER redox alterations and early ER-stress-related signaling events induced by acetaminophen, such as ER glutathione depletion, phosphorylation of eIF2alpha and JNK and induction of the transcription factor GADD153, were not counteracted by co-treatment with BGP-15.
Phosphorylation (phosphorylation) of eIF2alpha associated with stress and paracetamol
2) Confidence 0.80 Published 2010 Journal Toxicol. Appl. Pharmacol. Section Abstract Doc Link 19931551 Disease Relevance 1.01 Pain Relevance 0.63
Interestingly, pranoprofen alone induced eIF2alpha phosphorylation, which was further increased by ER stress.
Phosphorylation (phosphorylation) of eIF2alpha associated with stress
3) Confidence 0.80 Published 2009 Journal Neurochem. Int. Section Abstract Doc Link 19114067 Disease Relevance 1.29 Pain Relevance 0.15
ER stress-induced phosphorylation of alpha-subunit of eukaryotic initiation factor-2 (eIF2alpha) has been reported to be involved in CHOP induction.
Phosphorylation (phosphorylation) of eIF2alpha associated with stress
4) Confidence 0.79 Published 2009 Journal Neurochem. Int. Section Abstract Doc Link 19114067 Disease Relevance 1.32 Pain Relevance 0.17
However, if the eIF-2 has previously been phosphorylated by the reticulocyte heme-controlled repressor, the 40S subunit induced inhibition cannot be reversed by elimination of free GDP.
Phosphorylation (phosphorylated) of eIF-2 in reticulocyte
5) Confidence 0.51 Published 1983 Journal Biochemistry Section Abstract Doc Link 6551177 Disease Relevance 0.16 Pain Relevance 0.08
The instability of initiation complexes containing eIF-2, together with the impairment of guanine nucleotide exchange after phosphorylation of eIF-2 [Clemens, M.J., Pain, V.M., Wong, S.
Phosphorylation (phosphorylation) of eIF-2 associated with pain
6) Confidence 0.51 Published 1983 Journal Biochemistry Section Abstract Doc Link 6551177 Disease Relevance 0.17 Pain Relevance 0.10
Assembly and breakdown of mammalian protein synthesis initiation complexes: regulation by guanine nucleotides and by phosphorylation of initiation factor eIF-2.
Phosphorylation (phosphorylation) of eIF-2
7) Confidence 0.51 Published 1983 Journal Biochemistry Section Title Doc Link 6551177 Disease Relevance 0.14 Pain Relevance 0.05
The instability of initiation complexes containing eIF-2, together with the impairment of guanine nucleotide exchange after phosphorylation of eIF-2 [Clemens, M.J., Pain, V.M., Wong, S.
Phosphorylation (phosphorylation) of eIF-2 associated with pain
8) Confidence 0.50 Published 1983 Journal Biochemistry Section Abstract Doc Link 6551177 Disease Relevance 0.18 Pain Relevance 0.10
The protein expression and phosphorylation state of the eukaryotic translation initiation factor 2 alpha (eIF2?)
Phosphorylation (phosphorylation) of eukaryotic translation initiation factor 2 alpha
9) Confidence 0.42 Published 2010 Journal PLoS ONE Section Body Doc Link PMC3004931 Disease Relevance 0.32 Pain Relevance 0
Furthermore, the inability of GEF to utilize eIF-2 (alpha P) X GDP explains how phosphorylation of eIF-2 can inhibit polypeptide chain initiation.
Phosphorylation (phosphorylation) of eIF-2
10) Confidence 0.29 Published 1983 Journal J. Biol. Chem. Section Abstract Doc Link 6553052 Disease Relevance 0.07 Pain Relevance 0
The factor also stimulated markedly the rate of ternary complex formation using eIF-2 X GDP as substrate with GTP and Met-tRNAi but not using phosphorylated eIF-2 X GDP as substrate. eIF-2 is released from the 80 S initiation complex with hydrolysis of GTP.
Neg (not) Phosphorylation (phosphorylated) of eIF-2
11) Confidence 0.22 Published 1983 Journal J. Biol. Chem. Section Abstract Doc Link 6553052 Disease Relevance 0.14 Pain Relevance 0.06
Purified GEF increased the rate of exchange of [32P] GDP for unlabeled GDP 25-fold but did not function with phosphorylated eIF-2 (alpha subunit).
Phosphorylation (phosphorylated) of eIF-2
12) Confidence 0.19 Published 1983 Journal J. Biol. Chem. Section Abstract Doc Link 6553052 Disease Relevance 0.14 Pain Relevance 0.07

General Comments

This test has worked.

Personal tools
Namespaces

Variants
Actions
Navigation
Toolbox