INT227872

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Context Info
Confidence 0.01
First Reported 2008
Last Reported 2010
Negated 0
Speculated 0
Reported most in Body
Documents 7
Total Number 9
Disease Relevance 2.44
Pain Relevance 0.19

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

methyltransferase activity (MLL) nucleus (MLL) protein complex assembly (MLL)
DNA binding (MLL)
MLL (Homo sapiens)
Pain Link Frequency Relevance Heat
Glutamate 10 91.80 High High
Glutamate receptor 10 84.80 Quite High
anesthesia 13 63.76 Quite High
Potency 15 5.00 Very Low Very Low Very Low
isoflurane 6 5.00 Very Low Very Low Very Low
Central nervous system 3 5.00 Very Low Very Low Very Low
medulla 3 5.00 Very Low Very Low Very Low
Pain 2 5.00 Very Low Very Low Very Low
Disease Link Frequency Relevance Heat
Cockayne Syndrome 275 98.88 Very High Very High Very High
Targeted Disruption 10 98.10 Very High Very High Very High
Visceral Leishmaniasis 94 89.52 High High
Contagious Ecthyma 31 84.40 Quite High
Tumor Necrosis Factor Receptor-associated Periodic Syndrome 5 83.20 Quite High
Infection 169 75.88 Quite High
Hutchinson-gilford Progeria Syndrome 20 68.96 Quite High
Skin Cancer 5 51.28 Quite High
Disease 83 48.96 Quite Low
Viral Meningitis 33 48.64 Quite Low

Sentences Mentioned In

Key: Protein Mutation Event Anatomy Negation Speculation Pain term Disease term
Each step, from the interaction of the receptor-binding protein with its receptor and the subsequent triggering of the fusion protein, to the conformational changes in the fusion protein that lead to fusion readiness, and the refolding of the fusion protein that drives membrane merger, are potential targets for antiviral compounds.
Positive_regulation (triggering) of fusion protein
1) Confidence 0.01 Published 2010 Journal PLoS Pathogens Section Body Doc Link PMC2965769 Disease Relevance 0.07 Pain Relevance 0
The peptides were present during the entire fusion process, allowing them to act at the stages of triggering/activation of the fusion protein, or during subsequent fusion.
Positive_regulation (activation) of fusion protein
2) Confidence 0.01 Published 2010 Journal PLoS Pathogens Section Body Doc Link PMC2965769 Disease Relevance 0.08 Pain Relevance 0
The peptides were present during the entire fusion process, allowing them to act at the stages of triggering/activation of the fusion protein, or during subsequent fusion.
Positive_regulation (triggering) of fusion protein
3) Confidence 0.01 Published 2010 Journal PLoS Pathogens Section Body Doc Link PMC2965769 Disease Relevance 0.08 Pain Relevance 0
We utilized this information and incorporated multiple tandem repeat regions of haspb1 and LdK39 in order to increase the antigen epitope density within the resulting fusion protein.
Positive_regulation (increase) of fusion protein
4) Confidence 0.01 Published 2010 Journal PLoS Neglected Tropical Diseases Section Body Doc Link PMC2939046 Disease Relevance 0.53 Pain Relevance 0
terminal exon to generate a CSB-PGBD3 fusion protein.
Positive_regulation (generate) of fusion protein
5) Confidence 0.01 Published 2008 Journal PLoS Genetics Section Body Doc Link PMC2268245 Disease Relevance 0.05 Pain Relevance 0
Insertion of an element with these features into a host intron can generate an N-terminal fusion protein as observed for the PGBD3 insertion into CSB intron 5 (Figure 1).
Positive_regulation (generate) of fusion protein
6) Confidence 0.01 Published 2008 Journal PLoS Genetics Section Body Doc Link PMC2268245 Disease Relevance 0.16 Pain Relevance 0
According to this hypothesis, mutations downstream of CSB exon 5 would cause CS by impairing expression of functional CSB without affecting expression of the fusion protein; nonsense and frameshift mutations upstream of exon 6 would not cause CS [33] because they would also abolish expression of the fusion protein; mutations that do cause CS would be recessive because functional CSB masks the effects of the CSB-PGBD3 fusion protein; and mouse models of severe CSB mutations or a CSA knockout would not exhibit the full range of CS symptoms because rodents lack the PGBD3 insertion that generates the CSB-PGBD3 fusion protein.
Positive_regulation (generates) of fusion protein associated with targeted disruption and cockayne syndrome
7) Confidence 0.01 Published 2008 Journal PLoS Genetics Section Body Doc Link PMC2268245 Disease Relevance 0.89 Pain Relevance 0.06
We provide a combination of genomic, genetic, mRNA, and protein evidence that a CSB-PGBD3 fusion protein, generated by alternative splicing of CSB exon 5 to a PGBD3 transposon within intron 5, is a major product of the CSB/PGBD3 locus; that the fusion protein has been highly conserved in primates since the transposon was domesticated at least 43 Mya; that the fusion protein continues to be expressed in primary cells from three CS patients who lack functional CSB; and that nearly all CS-causing CSB mutations are located downstream of the exon 5/6 boundary in the ATPase and C-terminal domains of CSB protein, with the result that the fusion protein is predicted to be expressed in at least 21 of 24 characterized CS cell lines lacking functional CSB.
Positive_regulation (generated) of fusion protein associated with cockayne syndrome
8) Confidence 0.01 Published 2008 Journal PLoS Genetics Section Body Doc Link PMC2268245 Disease Relevance 0.31 Pain Relevance 0.13
Moreover, the CSB and PGBD3 coding regions are in frame across this splice junction, suggesting that transcripts initiating at a normal CSB promoter could be alternatively spliced to the PiggyBac element instead of exon 6, thus generating a CSB-PGBD3 fusion protein ( 1B).
Positive_regulation (generating) of fusion protein
9) Confidence 0.01 Published 2008 Journal PLoS Genetics Section Body Doc Link PMC2268245 Disease Relevance 0.28 Pain Relevance 0

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