INT339845

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Context Info
Confidence 0.23
First Reported 2010
Last Reported 2010
Negated 0
Speculated 0
Reported most in Body
Documents 1
Total Number 4
Disease Relevance 0.31
Pain Relevance 0.20

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

cell proliferation (UCN2) extracellular space (UCN2) extracellular region (UCN2)
response to stress (UCN2)
UCN2 (Homo sapiens)
Pain Link Frequency Relevance Heat
imagery 4 77.76 Quite High
Inflammation 24 70.56 Quite High
tolerance 28 5.00 Very Low Very Low Very Low
rheumatoid arthritis 12 5.00 Very Low Very Low Very Low
cytokine 8 5.00 Very Low Very Low Very Low
Sicca syndrome 8 5.00 Very Low Very Low Very Low
Osteoarthritis 8 5.00 Very Low Very Low Very Low
Inflammatory mediators 4 5.00 Very Low Very Low Very Low
IPN 4 5.00 Very Low Very Low Very Low
Arthritis 4 5.00 Very Low Very Low Very Low
Disease Link Frequency Relevance Heat
INFLAMMATION 20 70.56 Quite High
Myositis 4 55.68 Quite High
Dermatomyositis 36 41.68 Quite Low
Apoptosis 32 25.72 Quite Low
Rheumatic Diseases 20 5.00 Very Low Very Low Very Low
Rheumatoid Arthritis 12 5.00 Very Low Very Low Very Low
Arthritis 8 5.00 Very Low Very Low Very Low
Systemic Lupus Erythematosus 8 5.00 Very Low Very Low Very Low
Autoimmune Disease 8 5.00 Very Low Very Low Very Low
Syndrome 8 5.00 Very Low Very Low Very Low

Sentences Mentioned In

Key: Protein Mutation Event Anatomy Negation Speculation Pain term Disease term
-stimulated Jurkat cells were evaluated by WB using antibodies against SRP72, SRP54 (nonphosphorylated form of SRP), and GAPDH (loading control).
Phosphorylation (nonphosphorylated) of SRP
1) Confidence 0.23 Published 2010 Journal The Journal of Biological Chemistry Section Body Doc Link PMC2963399 Disease Relevance 0 Pain Relevance 0
g/ml) to human SRP72 epitope mapping near the C terminus of SRP72 of human origin (Santa Cruz Biotechnology, 1:2500), human SRP54 (Sigma) (1:2500), which represents the nonphosphorylated SRP protein and human GAPDH (Syd Labs, Boston) (1:3000).
Phosphorylation (nonphosphorylated) of SRP
2) Confidence 0.22 Published 2010 Journal The Journal of Biological Chemistry Section Body Doc Link PMC2963399 Disease Relevance 0 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 SRP
3) Confidence 0.17 Published 2010 Journal The Journal of Biological Chemistry Section Body Doc Link PMC2963399 Disease Relevance 0.14 Pain Relevance 0.07
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 SRP
4) Confidence 0.17 Published 2010 Journal The Journal of Biological Chemistry Section Body Doc Link PMC2963399 Disease Relevance 0.18 Pain Relevance 0.09

General Comments

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