INT86584

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Context Info
Confidence 0.80
First Reported 2000
Last Reported 2009
Negated 0
Speculated 0
Reported most in Body
Documents 10
Total Number 11
Disease Relevance 4.99
Pain Relevance 0.41

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

extracellular space (S100A8) extracellular region (S100A8) plasma membrane (S100A8)
cytoskeleton (S100A8) cytoplasm (S100A8)
Anatomy Link Frequency
epithelial cells 2
AGS 1
S100A8 (Homo sapiens)
Pain Link Frequency Relevance Heat
peptic ulcer disease 9 98.24 Very High Very High Very High
Inflammation 28 90.08 High High
agonist 12 5.00 Very Low Very Low Very Low
abdominal pain 9 5.00 Very Low Very Low Very Low
addiction 9 5.00 Very Low Very Low Very Low
TRP channel 6 5.00 Very Low Very Low Very Low
antagonist 6 5.00 Very Low Very Low Very Low
Inflammatory response 6 5.00 Very Low Very Low Very Low
nud 5 5.00 Very Low Very Low Very Low
Inflammatory mediators 3 5.00 Very Low Very Low Very Low
Disease Link Frequency Relevance Heat
Adhesions 27 100.00 Very High Very High Very High
Ulcers 19 99.98 Very High Very High Very High
Stomach Cancer 25 99.12 Very High Very High Very High
Alagille Syndrome 3 99.12 Very High Very High Very High
Infection 46 98.32 Very High Very High Very High
Disease 82 98.24 Very High Very High Very High
Sprains And Strains 79 94.32 High High
Lymphatic System Cancer 8 93.04 High High
Adenocarcinoma 9 92.32 High High
INFLAMMATION 37 90.08 High High

Sentences Mentioned In

Key: Protein Mutation Event Anatomy Negation Speculation Pain term Disease term
CagA is tyrosine-phosphorylated and induces changes in the tyrosine phosphorylation state of distinct cellular proteins.
Phosphorylation (phosphorylated) of CagA
1) Confidence 0.80 Published 2000 Journal Science Section Abstract Doc Link 10688800 Disease Relevance 0.87 Pain Relevance 0.13
Recent study clearly confirmed that almost one dozen of factors such as SHP-1, Grd2, Grb2, phosphatidylinositol 3-OH kinase (PI3K), have also binding abilities to CagA phosphorylation sites [34].
Phosphorylation (phosphorylation) of CagA
2) Confidence 0.80 Published 2009 Journal PLoS ONE Section Body Doc Link PMC2768901 Disease Relevance 0.28 Pain Relevance 0
Upon translocation, CagA is tyrosine phosphorylated by Src family kinases (SFKs), which themselves become inactivated via a negative feedback loop.
Phosphorylation (phosphorylated) of CagA
3) Confidence 0.80 Published 2007 Journal Cell. Microbiol. Section Abstract Doc Link 17217431 Disease Relevance 0.86 Pain Relevance 0.10
Here, we show that tyrosine-phosphorylated CagA disrupts adhesion of AGS cells to the extracellular matrix.
Phosphorylation (phosphorylated) of CagA in AGS associated with alagille syndrome and adhesions
4) Confidence 0.80 Published 2007 Journal Cell. Microbiol. Section Abstract Doc Link 17217431 Disease Relevance 0.97 Pain Relevance 0.09
The Helicobacter pylori CagA protein disrupts matrix adhesion of gastric epithelial cells by dephosphorylation of vinculin.
Phosphorylation (dephosphorylation) of CagA in epithelial cells associated with ulcers and adhesions
5) Confidence 0.79 Published 2007 Journal Cell. Microbiol. Section Title Doc Link 17217431 Disease Relevance 1.01 Pain Relevance 0.09
The CagA gene is found in the Cag pathogenic island (PAI), a genome segment of 40 kb that encodes approximately 30 genes.[18] CagA PAI genes are thought to encode a complex syringe-like structure called type IV secretary complex that helps in translocating the CagA protein into the gastric epithelial cells.[19–21] After translocation, CagA is phosphorylated, possibly by known oncogenes[22] and causes rearrangement of the host cytoskeleton and alters cell signaling[18] and perturbs cell cycle control,[23] which are important pathogenic mechanisms of gastroduodenal disease.
Phosphorylation (phosphorylated) of CagA in epithelial cells associated with disease
6) Confidence 0.61 Published 2009 Journal Saudi Journal of Gastroenterology : Official Journal of the Saudi Gastroenterology Association Section Body Doc Link PMC2702974 Disease Relevance 0.69 Pain Relevance 0
Finally, sequences are annotated according to segments (20–50 amino acids) flanking the EPIYA motifs (segments EPIYA-A, -B, -C, or –D) [20–23], after the identification of the essential CagA phosphorylation sites as confirmed by mutagenesis during infection and transfection [24].
Phosphorylation (phosphorylation) of CagA associated with infection
7) Confidence 0.61 Published 2009 Journal PLoS ONE Section Body Doc Link PMC2768901 Disease Relevance 0.16 Pain Relevance 0
A phosphorylation-independent mechanism for CagA intracellular effects has also been proposed.
Phosphorylation (phosphorylation) of CagA
8) Confidence 0.61 Published 2004 Journal Curr. Opin. Gastroenterol. Section Body Doc Link 15703688 Disease Relevance 0.16 Pain Relevance 0
When an extracellular, Ca2+-independent stimulus is used, S100A9 proteins, which are markedly phosphorylated, and S100A8 proteins, which are phosphorylated weakly, do not translocate [153], indicating that phosphorylation is strictly dependent on Ca2+ influx.
Phosphorylation (phosphorylated) of S100A8
9) Confidence 0.51 Published 2008 Journal J Leukoc Biol Section Body Doc Link PMC2567897 Disease Relevance 0 Pain Relevance 0
As fMLF stimulation mediates a significant increase in S100A9 localized to the base of lamellipodia and as phosphorylated S100A8/S100A9 associates with F-actin, it can be assumed that phosphorylation results in S100A9 translocation.
Phosphorylation (phosphorylated) of S100A8
10) Confidence 0.51 Published 2008 Journal J Leukoc Biol Section Body Doc Link PMC2567897 Disease Relevance 0 Pain Relevance 0
When an extracellular, Ca2+-independent stimulus is used, S100A9 proteins, which are markedly phosphorylated, and S100A8 proteins, which are phosphorylated weakly, do not translocate [153], indicating that phosphorylation is strictly dependent on Ca2+ influx.
Phosphorylation (phosphorylated) of S100A8
11) Confidence 0.39 Published 2008 Journal J Leukoc Biol Section Body Doc Link PMC2567897 Disease Relevance 0 Pain Relevance 0

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