INT110772

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Context Info
Confidence 0.32
First Reported 2003
Last Reported 2010
Negated 0
Speculated 0
Reported most in Body
Documents 2
Total Number 8
Disease Relevance 1.12
Pain Relevance 0.30

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

Golgi apparatus (Tjp1) plasma membrane (Tjp1) nucleus (Tjp1)
cytoplasm (Tjp1)
Anatomy Link Frequency
blood vessels 1
bridge 1
brain 1
Tjp1 (Rattus norvegicus)
Pain Link Frequency Relevance Heat
peptic ulcer disease 1 97.96 Very High Very High Very High
ischemia 35 86.72 High High
Intracerebroventricular 7 58.40 Quite High
Central nervous system 28 34.60 Quite Low
cva 7 21.44 Low Low
imagery 14 5.00 Very Low Very Low Very Low
ketamine 7 5.00 Very Low Very Low Very Low
anesthesia 7 5.00 Very Low Very Low Very Low
Multiple sclerosis 7 5.00 Very Low Very Low Very Low
Disease Link Frequency Relevance Heat
Stomach Cancer 1 98.84 Very High Very High Very High
Adhesions 1 98.32 Very High Very High Very High
Disease 8 97.96 Very High Very High Very High
Ulcers 3 97.64 Very High Very High Very High
Brain Hemorrhage 14 87.92 High High
Osteoarthritis 14 82.08 Quite High
Targeted Disruption 7 54.32 Quite High
Hypoxia 21 44.88 Quite Low
Brain Tumor 14 41.88 Quite Low
Cv General 4 Under Development 14 37.28 Quite Low

Sentences Mentioned In

Key: Protein Mutation Event Anatomy Negation Speculation Pain term Disease term
However, using immunoprecipitation analysis we show that the interaction of occludin and ZO-1 is reduced in the brain regions treated with ultrasound (Figure 3B).


ZO-1 Binding (interaction) of in brain
1) Confidence 0.32 Published 2010 Journal BMC Neurol Section Body Doc Link PMC3020671 Disease Relevance 0 Pain Relevance 0
Given that the phosphorylation of the proteins is an immediate event and the disruption of the BBB also occurs shortly after sonication, it is plausible that the ultrasound-mediated diminished interaction of occludin and ZO-1 is due to alteration in phosphorylation level of tight junction proteins.
ZO-1 Binding (interaction) of
2) Confidence 0.32 Published 2010 Journal BMC Neurol Section Body Doc Link PMC3020671 Disease Relevance 0.07 Pain Relevance 0.04
The intracellular domain of these proteins interact with cytoplasmic membrane-associated tight junction proteins called zonula occludens (ZO proteins), which act as a bridge between integral membrane proteins and the actin cytoskeleton [1,5].
occludens Binding (interact) of in bridge
3) Confidence 0.28 Published 2010 Journal BMC Neurol Section Body Doc Link PMC3020671 Disease Relevance 0 Pain Relevance 0
The interaction of occludin and ZO-1 is required for proper functioning of the tight junctions and is also subject to tight regulation by several mechanisms [1,35].
ZO-1 Binding (interaction) of
4) Confidence 0.24 Published 2010 Journal BMC Neurol Section Body Doc Link PMC3020671 Disease Relevance 0.05 Pain Relevance 0.03
It has been shown that the post-translational modifications play an essential role in controlling the interaction of occludin and ZO-1.
ZO-1 Binding (interaction) of
5) Confidence 0.24 Published 2010 Journal BMC Neurol Section Body Doc Link PMC3020671 Disease Relevance 0.07 Pain Relevance 0.04
Our data provides evidence that focused ultrasound in the presence of circulating ultrasound contrast agents (microbubbles) disrupts the interaction of tight junction proteins (occludin and ZO-1), thus affecting the integrity of the BBB.
ZO-1 Binding (interaction) of
6) Confidence 0.24 Published 2010 Journal BMC Neurol Section Body Doc Link PMC3020671 Disease Relevance 0.27 Pain Relevance 0.06
There are several reports indicating that the phosphorylation of occludin at tyrosine residues (Tyr-398 and Tyr-402) decreases the interaction of this protein with ZO-1, ZO-2 and ZO-3, thus enhancing the permeability of the blood vessels [36,37].
ZO-1 Binding (interaction) of in blood vessels
7) Confidence 0.24 Published 2010 Journal BMC Neurol Section Body Doc Link PMC3020671 Disease Relevance 0.09 Pain Relevance 0.04
We show that injected CagA associates with the epithelial tight-junction scaffolding protein ZO-1 and the transmembrane protein junctional adhesion molecule, causing an ectopic assembly of tight-junction components at sites of bacterial attachment, and altering the composition and function of the apical-junctional complex.
ZO-1 Binding (associates) of associated with adhesions
8) Confidence 0.17 Published 2003 Journal Science Section Abstract Doc Link 12775840 Disease Relevance 0.56 Pain Relevance 0.10

General Comments

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