INT228088

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Context Info
Confidence 0.54
First Reported 2008
Last Reported 2010
Negated 0
Speculated 0
Reported most in Body
Documents 6
Total Number 7
Disease Relevance 4.64
Pain Relevance 0.85

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

signal transduction (Ceacam1) plasma membrane (Ceacam1)
Anatomy Link Frequency
memory B cells 2
Plasma cells 1
cleavage 1
Ceacam1 (Mus musculus)
Pain Link Frequency Relevance Heat
Demyelination 246 98.88 Very High Very High Very High
Inflammation 100 98.28 Very High Very High Very High
cytokine 37 95.52 Very High Very High Very High
Inflammatory response 5 81.36 Quite High
chemokine 4 68.00 Quite High
Spinal cord 66 62.48 Quite High
Central nervous system 70 54.60 Quite High
Multiple sclerosis 44 43.20 Quite Low
metalloproteinase 1 35.28 Quite Low
Neuritis 34 26.32 Quite Low
Disease Link Frequency Relevance Heat
Hepatitis 14 99.68 Very High Very High Very High
Demyelinating Disease 458 98.88 Very High Very High Very High
Epstein-barr Virus 71 98.88 Very High Very High Very High
INFLAMMATION 105 98.28 Very High Very High Very High
Infection 272 98.24 Very High Very High Very High
Hypergammaglobulinemia 1 96.80 Very High Very High Very High
Viral Meningitis 28 91.12 High High
Adhesions 3 82.40 Quite High
Sprains And Strains 168 81.44 Quite High
Viremia 1 75.44 Quite High

Sentences Mentioned In

Key: Protein Mutation Event Anatomy Negation Speculation Pain term Disease term
As demonstrated in Figure 2, the top networks identified by IPA at 6 hours after pneumonectomy are associated with cell-cell signaling (including up-regulation of Ceacam1 and ItgaV - Figure 2A), and inhibition of inflammatory cell migration (down-regulation of the pro-inflammatory cytokines Cxcl1 and Cxcl10, as well as Nf??
Localization (regulation) of Ceacam1 associated with inflammation and cytokine
1) Confidence 0.54 Published 2009 Journal Respir Res Section Body Doc Link PMC2770038 Disease Relevance 0.43 Pain Relevance 0.22
They also differ in their cleavage signal site whereby MHV-A59 S is cleaved posttranslationally into S1 and S2 subunits, but MHV-2 S protein is not cleaved and unable to cause fusion in vivo and in vitro.
Localization (cleaved) of MHV-A59 in cleavage
2) Confidence 0.33 Published 2010 Journal Interdisciplinary Perspectives on Infectious Diseases Section Body Doc Link PMC2905936 Disease Relevance 0.73 Pain Relevance 0.10
To avoid a high mortality rate of MHV-2 due to hepatitis, 0.5?
Localization (rate) of MHV-2 associated with hepatitis
3) Confidence 0.31 Published 2010 Journal Interdisciplinary Perspectives on Infectious Diseases Section Body Doc Link PMC2905936 Disease Relevance 1.45 Pain Relevance 0.50
Plasma cells account for the majority of MHV68 reactivation from explanted splenocytes
Localization (reactivation) of MHV68 in Plasma cells
4) Confidence 0.06 Published 2009 Journal PLoS Pathogens Section Body Doc Link PMC2777334 Disease Relevance 0.27 Pain Relevance 0
Following cell lysis with proteinase K, two rounds of nested PCR were performed on each sample to detect the presence of the MHV68 ORF50.
Localization (presence) of MHV68
5) Confidence 0.06 Published 2009 Journal PLoS Pathogens Section Body Doc Link PMC2777334 Disease Relevance 0 Pain Relevance 0
Analyses of virus latency in the spleen have shown that during the establishment of latency MHV68 is found in naive, germinal center and memory B cells [14],[18].
Localization (found) of MHV68 in memory B cells
6) Confidence 0.06 Published 2009 Journal PLoS Pathogens Section Body Doc Link PMC2777334 Disease Relevance 0.63 Pain Relevance 0
Similar to EBV pathogenesis, memory B cells are the primary long-term reservoir of latent MHV68 in mice [7],[8],[9].
Localization (reservoir) of MHV68 in memory B cells associated with epstein-barr virus
7) Confidence 0.02 Published 2008 Journal PLoS Pathogens Section Body Doc Link PMC2270344 Disease Relevance 1.13 Pain Relevance 0.03

General Comments

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