INT189881

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Context Info
Confidence 0.36
First Reported 2006
Last Reported 2010
Negated 1
Speculated 0
Reported most in Body
Documents 6
Total Number 9
Disease Relevance 1.24
Pain Relevance 0.04

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) Golgi apparatus (Cdh1) plasma membrane (Cdh1)
cytoplasm (Cdh1)
Anatomy Link Frequency
plasma 2
pancreatic beta cells 1
lateral 1
epithelial cells 1
intestine 1
Cdh1 (Rattus norvegicus)
Pain Link Frequency Relevance Heat
Central nervous system 5 86.40 High High
anesthesia 13 5.00 Very Low Very Low Very Low
Dopamine 8 5.00 Very Low Very Low Very Low
isoflurane 8 5.00 Very Low Very Low Very Low
imagery 8 5.00 Very Low Very Low Very Low
ketamine 4 5.00 Very Low Very Low Very Low
Pain 4 5.00 Very Low Very Low Very Low
agonist 4 5.00 Very Low Very Low Very Low
Disease Link Frequency Relevance Heat
Disease 16 96.96 Very High Very High Very High
Coronary Artery Disease 72 94.20 High High
Adhesions 134 83.72 Quite High
Apoptosis 20 49.56 Quite Low
Targeted Disruption 16 8.00 Low Low
Infection 84 5.00 Very Low Very Low Very Low
Sprains And Strains 32 5.00 Very Low Very Low Very Low
Sepsis 8 5.00 Very Low Very Low Very Low
Gastroenteritis 4 5.00 Very Low Very Low Very Low
Ulcers 4 5.00 Very Low Very Low Very Low

Sentences Mentioned In

Key: Protein Mutation Event Anatomy Negation Speculation Pain term Disease term
In addition, it was reported that E-cadherin that had not bound to catenin complex was not transported to the plasma membrane, but was instead degraded in lysosomes [16].
E-cadherin Neg (not) Binding (bound) of in plasma
1) Confidence 0.36 Published 2010 Journal Acta Histochemica et Cytochemica Section Body Doc Link PMC2875860 Disease Relevance 0.21 Pain Relevance 0
These results show that exogenous E-cadherin does not affect prolactin mRNA transcription; rather, it decreases the protein content of prolactin.
E-cadherin Binding (exogenous) of
2) Confidence 0.28 Published 2010 Journal Acta Histochemica et Cytochemica Section Body Doc Link PMC2875860 Disease Relevance 0.39 Pain Relevance 0
It has been reported that nascent E-cadherin binds to catenin complex to expedite transport from the Golgi network to the plasma membrane [13].
E-cadherin Binding (binds) of in plasma
3) Confidence 0.28 Published 2010 Journal Acta Histochemica et Cytochemica Section Body Doc Link PMC2875860 Disease Relevance 0.27 Pain Relevance 0
If E-cadherin is located on hormone secretory granules, as is the case in pancreatic beta cells [2], the granules with E-cadherin not bound to catenin would be transported to lysosomes for degradation.
E-cadherin Binding (bound) of in pancreatic beta cells
4) Confidence 0.28 Published 2010 Journal Acta Histochemica et Cytochemica Section Body Doc Link PMC2875860 Disease Relevance 0.07 Pain Relevance 0
Future studies exploring the differences in how N-cadherin and E-cadherin interact with intracellular complexes will undoubtedly deepen our understanding of the roles of cadherin in histogenesis.
E-cadherin Binding (interact) of
5) Confidence 0.25 Published 2008 Journal Acta Histochemica et Cytochemica Section Body Doc Link PMC2576505 Disease Relevance 0 Pain Relevance 0.04
Alternatively, the process of tight junction formation and remodeling may involve interactions between tight junction proteins, the scaffolding protein ZO-1, and the E-cadherin complex that could result in E-cadherin exposure on the apical surface [75].
E-cadherin Binding (interactions) of
6) Confidence 0.06 Published 2006 Journal PLoS Pathogens Section Body Doc Link PMC1354196 Disease Relevance 0 Pain Relevance 0
By examining polarized epithelial monolayers in tissue culture and rabbit intestine in vivo, the authors investigate how and where L. monocytogenes breaches the tight junctions to interact with E-cadherin and invade.
E-cadherin Binding (interact) of in intestine
7) Confidence 0.06 Published 2006 Journal PLoS Pathogens Section Abstract Doc Link PMC1354196 Disease Relevance 0.07 Pain Relevance 0
This process depends on the interaction between the bacterial surface protein Internalin A and the host protein E-cadherin, located below the epithelial tight junctions at the lateral cell-to-cell contacts.
E-cadherin Binding (interaction) of in lateral
8) Confidence 0.06 Published 2006 Journal PLoS Pathogens Section Abstract Doc Link PMC1354196 Disease Relevance 0.10 Pain Relevance 0
It has long been known that Listeria monocytogenes invasion of epithelial cells requires binding of host cell E-cadherin, a cell-to-cell junction protein.
E-cadherin Binding (binding) of in epithelial cells
9) Confidence 0.06 Published 2006 Journal PLoS Pathogens Section Abstract Doc Link PMC1354196 Disease Relevance 0.15 Pain Relevance 0

General Comments

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