INT163489

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Context Info
Confidence 0.19
First Reported 2005
Last Reported 2011
Negated 0
Speculated 1
Reported most in Body
Documents 13
Total Number 14
Disease Relevance 8.63
Pain Relevance 0.35

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

endosome (CDH1) cell adhesion (CDH1) Golgi apparatus (CDH1)
plasma membrane (CDH1) cytoplasm (CDH1)
Anatomy Link Frequency
outflow 1
brain 1
epithelial cells 1
CDH1 (Homo sapiens)
Pain Link Frequency Relevance Heat
Inflammatory response 7 98.80 Very High Very High Very High
Bile 10 93.16 High High
headache 9 76.68 Quite High
Central nervous system 56 73.12 Quite High
antagonist 16 56.16 Quite High
Inflammation 59 33.56 Quite Low
Spinal cord 6 29.20 Quite Low
midbrain 6 26.48 Quite Low
medulla 28 22.76 Low Low
aspirin 21 5.00 Very Low Very Low Very Low
Disease Link Frequency Relevance Heat
Periodontitis 25 99.98 Very High Very High Very High
Breast Cancer 51 99.80 Very High Very High Very High
Metastasis 16 99.66 Very High Very High Very High
Diarrhoea 23 99.44 Very High Very High Very High
Stomach Cancer 94 99.02 Very High Very High Very High
INFLAMMATION 62 98.80 Very High Very High Very High
Adenoma 4 98.24 Very High Very High Very High
Meningioma 7 97.88 Very High Very High Very High
Carcinoma 5 97.80 Very High Very High Very High
Adhesions 20 97.42 Very High Very High Very High

Sentences Mentioned In

Key: Protein Mutation Event Anatomy Negation Speculation Pain term Disease term
In addition, L. monocytogenes has evolved species-specific strategies for intestinal entry by exploiting the interaction between the internalin protein and its receptor E-cadherin, or inducing diarrhea and an inflammatory response via the activity of its hemolytic toxin, listeriolysin.
E-cadherin Binding (interaction) of associated with inflammatory response and diarrhoea
1) Confidence 0.19 Published 2009 Journal Curr. Top. Microbiol. Immunol. Section Abstract Doc Link 19812983 Disease Relevance 1.03 Pain Relevance 0.22
Similarly the metastasis suppressor gene E-cadherin (CDH1), which binds to ?
CDH1 Binding (binds) of associated with metastasis
2) Confidence 0.17 Published 2008 Journal Current Medicinal Chemistry Section Body Doc Link PMC2764862 Disease Relevance 0.85 Pain Relevance 0
Similarly the metastasis suppressor gene E-cadherin (CDH1), which binds to ?
E-cadherin Binding (binds) of associated with metastasis
3) Confidence 0.17 Published 2008 Journal Current Medicinal Chemistry Section Body Doc Link PMC2764862 Disease Relevance 0.86 Pain Relevance 0
E-cadherin functions in AG cells to bind the arachnoid cells lining the arachnoid villi and granulations together flexibly and may allow the formation of extracellular cisterns during the bulk outflow of CSF [20].
E-cadherin Binding (bind) of in outflow
4) Confidence 0.14 Published 2005 Journal Cerebrospinal Fluid Res Section Body Doc Link PMC1285366 Disease Relevance 0.26 Pain Relevance 0
The former interacts with E-cadherin, which is mostly expressed on epithelial cells in species-specific manner [175].
E-cadherin Binding (interacts) of in epithelial cells
5) Confidence 0.11 Published 2010 Journal Interdisciplinary Perspectives on Infectious Diseases Section Body Doc Link PMC2829626 Disease Relevance 0.38 Pain Relevance 0
All of these cases were concurrently positively associated with E-cadherin mutations [15].
E-cadherin Binding (associated) of
6) Confidence 0.10 Published 2006 Journal Diagn Pathol Section Body Doc Link PMC1475889 Disease Relevance 1.18 Pain Relevance 0
The relative risk of periodontitis associated with E-Cadherin and COX-2 was 0.1091(95% confidence interval: 0.005-0.2627) and 0.0485(95% confidence interval: 0.0066-0.3543), respectively.
E-Cadherin Binding (associated) of associated with periodontitis
7) Confidence 0.09 Published 2010 Journal J Transl Med Section Body Doc Link PMC2998472 Disease Relevance 0.63 Pain Relevance 0
Given that the endothelium and the choroid plexus epithelium of the blood-brain barrier may express E-cadherin [179, 233–235], some authors suggest that a receptor interaction between the cellular E-cadherin and bacterial internalin A might be the underlying mechanism of blood-brain-barrier crossing, similar to what happens at the intestinal and placental barrier [17, 21, 177, 212].
E-cadherin Spec (might) Binding (interaction) of in brain
8) Confidence 0.08 Published 2010 Journal Interdisciplinary Perspectives on Infectious Diseases Section Body Doc Link PMC2829626 Disease Relevance 0.32 Pain Relevance 0.10
Some similarities can be drawn with breast cancer: diffuse-type gastric cancers and lobular invasive breast carcinomas are both associated with E-cadherin loss, which is inversely correlated with HER2 amplification/overexpression which is more common in ductal invasive breast carcinomas and intestinal-type gastric cancers.
E-cadherin Binding (associated) of associated with breast cancer and stomach cancer
9) Confidence 0.06 Published 2011 Journal Pathology Research International Section Body Doc Link PMC3005843 Disease Relevance 1.49 Pain Relevance 0
MiR-200a targets the mRNA of the E-cadherin repressor proteins ZEB1(also known as Tcf8) and ZEB2 (also known as SIP1), subsequently increases the total E-cadherin available for binding to ?
E-cadherin Binding (binding) of
10) Confidence 0.06 Published 2010 Journal Mol Cancer Section Body Doc Link PMC2955614 Disease Relevance 0.29 Pain Relevance 0
However, Tyr654 phosphorylation results in dissociation of the E-cadherin/?
E-cadherin Binding (dissociation) of
11) Confidence 0.05 Published 2010 Journal Mol Cancer Section Body Doc Link PMC2955614 Disease Relevance 0.25 Pain Relevance 0
Disrupting the E-cadherin binding has been implicated in the transition form adenoma to carcinoma, suggesting that the adhesive role of ?
E-cadherin Binding (binding) of associated with adenoma and carcinoma
12) Confidence 0.03 Published 2006 Journal Invest New Drugs Section Body Doc Link PMC2780666 Disease Relevance 0.64 Pain Relevance 0.03
The InlA E-cadherin interaction is species-specific, and was shown to rely on a single amino acid residue in the E-cadherin molecule, which is prolin in permissive species such as humans, and glutamic acid in nonpermissive species such as the mouse [34].
E-cadherin Binding (interaction) of
13) Confidence 0.02 Published 2010 Journal International Journal of Inflammation Section Body Doc Link PMC3003996 Disease Relevance 0.29 Pain Relevance 0
Tight junctions are located most apically and are composed of junctional adhesion molecules (JAM), claudins and occludin, while adherens junctions lie just below the tight junctions and are formed by homotypic interactions of E-cadherin.
E-cadherin Binding (interactions) of associated with adhesions
14) Confidence 0.02 Published 2008 Journal PLoS Pathogens Section Body Doc Link PMC2323203 Disease Relevance 0.15 Pain Relevance 0

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