INT339853

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Context Info
Confidence 0.82
First Reported 2010
Last Reported 2010
Negated 0
Speculated 0
Reported most in Body
Documents 1
Total Number 23
Disease Relevance 5.39
Pain Relevance 1.30

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

cytosol (SRP72) nucleolus (SRP72) plasma membrane (SRP72)
translation (SRP72) cytoplasm (SRP72)
Anatomy Link Frequency
effector T cells 1
SRP72 (Homo sapiens)
Pain Link Frequency Relevance Heat
Sicca syndrome 46 98.72 Very High Very High Very High
tolerance 161 96.20 Very High Very High Very High
Inflammation 138 94.60 High High
Osteoarthritis 46 89.00 High High
rheumatoid arthritis 69 88.24 High High
Inflammatory mediators 23 81.56 Quite High
cytokine 46 80.32 Quite High
IPN 23 5.00 Very Low Very Low Very Low
Arthritis 23 5.00 Very Low Very Low Very Low
imagery 23 5.00 Very Low Very Low Very Low
Disease Link Frequency Relevance Heat
Syndrome 46 98.72 Very High Very High Very High
Systemic Lupus Erythematosus 46 97.88 Very High Very High Very High
Apoptosis 184 97.80 Very High Very High Very High
Dermatomyositis 207 97.22 Very High Very High Very High
INFLAMMATION 115 94.60 High High
Autoimmune Disease 46 94.16 High High
Cancer 23 92.32 High High
Arthritis 46 90.12 High High
Osteoarthritis 46 89.00 High High
Myositis 23 88.28 High High

Sentences Mentioned In

Key: Protein Mutation Event Anatomy Negation Speculation Pain term Disease term
Effects of p38 MAPK inhibitors (SB203580 and SB202190) on serine phosphorylation of SRP72 were examined in Jurkat cells stimulated by rhIL-1?.
Phosphorylation (phosphorylation) of SRP72
1) Confidence 0.82 Published 2010 Journal The Journal of Biological Chemistry Section Body Doc Link PMC2963399 Disease Relevance 0 Pain Relevance 0
-induced serine phosphorylation of SRP72 were examined using immunoprecipitates by anti-SRP19 antibodies.
Phosphorylation (phosphorylation) of SRP72
2) Confidence 0.82 Published 2010 Journal The Journal of Biological Chemistry Section Body Doc Link PMC2963399 Disease Relevance 0 Pain Relevance 0
These inhibitors dramatically reduced the SRP72 phosphorylation in a concentration-dependent manner (Fig. 3, C and E, respectively).
Phosphorylation (phosphorylation) of SRP72
3) Confidence 0.82 Published 2010 Journal The Journal of Biological Chemistry Section Body Doc Link PMC2963399 Disease Relevance 0 Pain Relevance 0
In contrast, phosphorylation of SRP54 was not observed, indicating an exclusive phosphorylation effect of SRP72 evaluated by anti-phosphoserine antibody.
Phosphorylation (phosphorylation) of SRP72
4) Confidence 0.82 Published 2010 Journal The Journal of Biological Chemistry Section Body Doc Link PMC2963399 Disease Relevance 0.06 Pain Relevance 0
induced phosphorylation of SRP72 (Fig. 3A, lanes 6–8).
Phosphorylation (phosphorylation) of SRP72
5) Confidence 0.82 Published 2010 Journal The Journal of Biological Chemistry Section Body Doc Link PMC2963399 Disease Relevance 0 Pain Relevance 0
Quantification of the SRP72 phosphorylation confirmed statistically significant reduction of SRP72 serine phosphorylation (Fig. 4, B and D, *, p < 0.05).
Phosphorylation (phosphorylation) of SRP72
6) Confidence 0.82 Published 2010 Journal The Journal of Biological Chemistry Section Body Doc Link PMC2963399 Disease Relevance 0 Pain Relevance 0
In 1998, it was reported that a serum from a patient with DM could immunoprecipitate the SRP complex from Jurkat cells metabolically labeled with [35S]methionine (36) or [32P]orthophosphate and that SRP72 is phosphorylated on a phosphoserine residue.
Phosphorylation (phosphorylated) of SRP72 associated with dermatomyositis
7) Confidence 0.82 Published 2010 Journal The Journal of Biological Chemistry Section Body Doc Link PMC2963399 Disease Relevance 0.54 Pain Relevance 0.08
on phosphorylation of SRP72 in Jurkat cells were evaluated by immunoprecipitating the SRP complex using anti-SRP19 antibodies followed by specific anti-phosphoserine antibodies in WB.
Phosphorylation (phosphorylation) of SRP72
8) Confidence 0.82 Published 2010 Journal The Journal of Biological Chemistry Section Body Doc Link PMC2963399 Disease Relevance 0 Pain Relevance 0
Quantification of the SRP72 phosphorylation confirmed statistically significant reduction of SRP72 serine phosphorylation (Fig. 4, B and D, *, p < 0.05).
Phosphorylation (phosphorylation) of SRP72
9) Confidence 0.82 Published 2010 Journal The Journal of Biological Chemistry Section Body Doc Link PMC2963399 Disease Relevance 0.05 Pain Relevance 0
Both inhibitors showed a concentration-dependent reduction of SRP72 phosphorylation (Fig. 4, A and C, *, p < 0.05).
Phosphorylation (phosphorylation) of SRP72
10) Confidence 0.82 Published 2010 Journal The Journal of Biological Chemistry Section Body Doc Link PMC2963399 Disease Relevance 0 Pain Relevance 0
Opposite the p38 MAPK inhibitors, JNK-MAPK pathway inhibitor SP600125 showed no effect on SRP72 phosphorylation in rhIL-1?
Phosphorylation (phosphorylation) of SRP72
11) Confidence 0.82 Published 2010 Journal The Journal of Biological Chemistry Section Body Doc Link PMC2963399 Disease Relevance 0.08 Pain Relevance 0
Our results confirmed that SRP72 was a phosphoprotein to which a serine residue is phosphorylated (25).
Phosphorylation (phosphorylated) of SRP72
12) Confidence 0.81 Published 2010 Journal The Journal of Biological Chemistry Section Body Doc Link PMC2963399 Disease Relevance 0.18 Pain Relevance 0.09
SRP72 is the only component in the SRP complex that can be phosphorylated.
Phosphorylation (phosphorylated) of SRP72
13) Confidence 0.81 Published 2010 Journal The Journal of Biological Chemistry Section Body Doc Link PMC2963399 Disease Relevance 0.18 Pain Relevance 0.09
causes up-regulation of protein expression and phosphorylation of SRP72 in Jurkat cells.
Phosphorylation (phosphorylation) of SRP72
14) Confidence 0.63 Published 2010 Journal The Journal of Biological Chemistry Section Body Doc Link PMC2963399 Disease Relevance 0.88 Pain Relevance 0.12
The aim of this study was to explore the pathways of phosphorylation and overexpression of the SRP72 polypeptide, using an in vitro model of Jurkat cells stimulated by recombinant human (rh)IL-1?
Phosphorylation (phosphorylation) of SRP72 polypeptide
15) Confidence 0.63 Published 2010 Journal The Journal of Biological Chemistry Section Abstract Doc Link PMC2963399 Disease Relevance 0 Pain Relevance 0.05
Results shown above indicated reduced SRP72 protein expression as well as reduced serine phosphorylation by MAPK inhibitors in rhIL-1?
Phosphorylation (phosphorylation) of SRP72 protein
16) Confidence 0.63 Published 2010 Journal The Journal of Biological Chemistry Section Body Doc Link PMC2963399 Disease Relevance 0.26 Pain Relevance 0
We suggest a few possible applications of this reaction on the cell physiology as follows. 1) It has been described that a GTPase domain on the docking protein for SRP at the rough ER could be related to the release of the complex SRP-docking-ribosome-mRNA-translocon (5, 24, 26–28). 2) The phosphorylation of the SRP72 might increase the affinity of SRP for its receptor on the rough ER membrane and facilitate the rough ER translocation of protein (5, 23, 29–31). 3) The phosphorylation of SRP72 influence on the SRP complex activity in general because of the targeting of the protein by SRP does not requires GTPase activity (31–35).
Phosphorylation (phosphorylation) of SRP72
17) Confidence 0.63 Published 2010 Journal The Journal of Biological Chemistry Section Body Doc Link PMC2963399 Disease Relevance 0.14 Pain Relevance 0.07
Our results show that phosphorylation of SRP72 is increased by rhIL-1?.
Phosphorylation (phosphorylation) of SRP72
18) Confidence 0.63 Published 2010 Journal The Journal of Biological Chemistry Section Body Doc Link PMC2963399 Disease Relevance 0.68 Pain Relevance 0.17
causes up-regulation of protein expression and phosphorylation of SRP72 in Jurkat cells.
Phosphorylation (phosphorylation) of SRP72
19) Confidence 0.63 Published 2010 Journal The Journal of Biological Chemistry Section Abstract Doc Link PMC2963399 Disease Relevance 0.14 Pain Relevance 0.04
We suggest a few possible applications of this reaction on the cell physiology as follows. 1) It has been described that a GTPase domain on the docking protein for SRP at the rough ER could be related to the release of the complex SRP-docking-ribosome-mRNA-translocon (5, 24, 26–28). 2) The phosphorylation of the SRP72 might increase the affinity of SRP for its receptor on the rough ER membrane and facilitate the rough ER translocation of protein (5, 23, 29–31). 3) The phosphorylation of SRP72 influence on the SRP complex activity in general because of the targeting of the protein by SRP does not requires GTPase activity (31–35).
Phosphorylation (phosphorylation) of SRP72
20) Confidence 0.63 Published 2010 Journal The Journal of Biological Chemistry Section Body Doc Link PMC2963399 Disease Relevance 0.18 Pain Relevance 0.09

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