INT208920

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Context Info
Confidence 0.61
First Reported 2007
Last Reported 2010
Negated 1
Speculated 3
Reported most in Body
Documents 6
Total Number 8
Disease Relevance 2.97
Pain Relevance 0.11

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

cytoskeletal protein binding (Ezr) cytosol (Ezr) nucleolus (Ezr)
plasma membrane (Ezr) cytoskeleton (Ezr) intracellular (Ezr)
Ezr (Mus musculus)
Pain Link Frequency Relevance Heat
Serotonin 1 98.84 Very High Very High Very High
Inflammation 28 73.52 Quite High
metalloproteinase 6 41.36 Quite Low
agonist 16 31.88 Quite Low
Chronic pancreatitis 66 20.56 Low Low
substance P 22 5.00 Very Low Very Low Very Low
Spinal cord 7 5.00 Very Low Very Low Very Low
antagonist 6 5.00 Very Low Very Low Very Low
Inflammatory response 4 5.00 Very Low Very Low Very Low
Inflammatory mediators 2 5.00 Very Low Very Low Very Low
Disease Link Frequency Relevance Heat
Cancer 166 99.32 Very High Very High Very High
Metastasis 246 98.64 Very High Very High Very High
Shock 2 93.14 High High
Adhesions 19 87.40 High High
Apoptosis 9 86.10 High High
Breast Cancer 12 78.32 Quite High
Rhabdomyosarcoma 12 76.64 Quite High
INFLAMMATION 33 73.52 Quite High
Glioma 6 72.36 Quite High
Pancreatic Cancer 132 68.08 Quite High

Sentences Mentioned In

Key: Protein Mutation Event Anatomy Negation Speculation Pain term Disease term
The flow cytometry assay further showed that changes in the ezrin protein level did not affect the cell cycle distribution (Figure 3B).
Regulation (changes) of ezrin protein
1) Confidence 0.61 Published 2010 Journal J Transl Med Section Body Doc Link PMC2916894 Disease Relevance 0.13 Pain Relevance 0
In addition, ezrin silencing might affect other signal pathway.
Spec (might) Regulation (affect) of ezrin
2) Confidence 0.45 Published 2010 Journal J Transl Med Section Body Doc Link PMC2916894 Disease Relevance 0.56 Pain Relevance 0
A series of experiments were conducted to determine the effect of different ezrin protein levels on the proliferation of MiaPaCa-2 cells in vitro.
Spec (determine) Regulation (effect) of ezrin protein
3) Confidence 0.27 Published 2010 Journal J Transl Med Section Body Doc Link PMC2916894 Disease Relevance 0.09 Pain Relevance 0
The change in the ezrin protein level had no significant effect on the cell growth rate in vitro (Figure 3A).
Regulation (change) of ezrin protein
4) Confidence 0.27 Published 2010 Journal J Transl Med Section Body Doc Link PMC2916894 Disease Relevance 0.08 Pain Relevance 0
Ezrin participates in several crucial signal transduction pathways, including the MAPK, AKT, Rho kinase and CD44 pathways, promoting cytoskeletal reorganization and subsequent morphogenetic alterations [3,5,8,11].
Regulation (participates) of Ezrin
5) Confidence 0.27 Published 2010 Journal J Transl Med Section Body Doc Link PMC2916894 Disease Relevance 0.71 Pain Relevance 0
Moreover, there were no obvious changes in the protein levels of Akt, phosphorylated-Akt and phosphorylated-ezrin (Tyr353) in both the ezrin silencing and the ezrin overexpression clones of MiaPaCa-2 cells (Figure 6).


Neg (no) Regulation (changes) of phosphorylated-ezrin
6) Confidence 0.24 Published 2010 Journal J Transl Med Section Body Doc Link PMC2916894 Disease Relevance 0.66 Pain Relevance 0
Therefore, it would be interesting to test whether ezrin is also involved in ?
Spec (whether) Regulation (involved) of ezrin
7) Confidence 0.08 Published 2010 Journal Journal of Receptor and Signal Transduction Research Section Body Doc Link PMC3018134 Disease Relevance 0 Pain Relevance 0
Overall NK1R-dependent genes were classified following the biological processes with which they are involved (GO anthology): apoptosis (GZMA, TNFRSF1B, TNFRSF1A, TRAF3, NOS2A, and BID); cell adhesion/hyaluronic acid binding (CD44 and AGC1); cell cycle (CCND2 and CCNG1); cell-cell signaling (FGF11 and GJA7); cytokinesis (CDC42 and KIF1B); development (FMR2); extracellular transporters & carriers (APOE); G-protein coupled receptors (GNA13 and PTGIR); growth factors (MXD1); heat shock proteins (PRNP, HSPH1, and HSPD1); immune response (BST-1, CTSW, and IL1R1); interferons (INFGR1) intracellular kinases (WBP6); intracellular transducers (MAP3K7); kinase activators & inhibitors (YWHAH); membrane channels (KCNAB1, KCNJ12, KCNQ1, and SLC30A4); nucleotide metabolism (PCSK1); oncogenes & tumor suppressors (BRCA1, MAP3K8, RET, VIL2, FLI1, MET, NF2, and VEGFR1); receptor mediated endocytosis (DAB2); receptor tyrosine kinase (EPHA2); regulation of transcription (NEUROD6); serotonin biosynthesis (YTPH1); symporters & antiporters (SLC16A1 and SLC1A1); transcription activators & repressors (FOXA1, HSF1, IER2, and NR1H2); and synaptic transmission (GRID1).


Regulation (regulation) of VIL2 associated with cancer, shock, apoptosis, serotonin and adhesions
8) Confidence 0.03 Published 2007 Journal BMC Urol Section Body Doc Link PMC1888709 Disease Relevance 0.73 Pain Relevance 0.11

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