INT66347

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Context Info
Confidence 0.65
First Reported 1996
Last Reported 2010
Negated 4
Speculated 0
Reported most in Body
Documents 29
Total Number 29
Disease Relevance 14.82
Pain Relevance 3.18

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)
Anatomy Link Frequency
CS1PV 2
eye 1
juvenile 1
sciatic nerve 1
U-2 OS 1
MLL (Homo sapiens)
Pain Link Frequency Relevance Heat
Sciatic nerve 3 99.90 Very High Very High Very High
Etanercept 3 99.86 Very High Very High Very High
rheumatoid arthritis 56 99.12 Very High Very High Very High
Adalimumab 3 98.80 Very High Very High Very High
Infliximab 4 98.16 Very High Very High Very High
anesthesia 37 98.04 Very High Very High Very High
Neuritis 15 95.84 Very High Very High Very High
Arthritis 3 94.64 High High
psoriasis 2 94.20 High High
spinal inflammation 2 93.60 High High
Disease Link Frequency Relevance Heat
Cockayne Syndrome 935 99.86 Very High Very High Very High
Disease 113 99.26 Very High Very High Very High
Rheumatoid Arthritis 56 99.12 Very High Very High Very High
Leukemia 5 98.12 Very High Very High Very High
Cancer 57 98.00 Very High Very High Very High
Diphtheria 6 97.76 Very High Very High Very High
Necrosis 2 97.76 Very High Very High Very High
Repression 18 97.64 Very High Very High Very High
Experimental Autoimmune Neuritis 4 95.84 Very High Very High Very High
Seronegative Spondarthritis 2 95.04 Very High Very High Very High

Sentences Mentioned In

Key: Protein Mutation Event Anatomy Negation Speculation Pain term Disease term
Like other MLL translocation products, the chimera MLL-ELL appears to play an important role in leukemogenesis [32], [33], [34], [35], [36].
Gene_expression (products) of MLL
1) Confidence 0.65 Published 2010 Journal PLoS ONE Section Body Doc Link PMC2955548 Disease Relevance 0.73 Pain Relevance 0.16
Etanercept is a recombinant fusion protein that can be used alone or in combination with other medications for conditions such as rheumatoid arthritis, juvenile rheumatoid arthritis, psoriatic arthritis, psoriasis, and ankylosing spondylitis.
Gene_expression (used) of fusion protein in juvenile associated with seronegative spondarthritis, spinal inflammation, psoriasis, rheumatoid arthritis, etanercept and arthritis
2) Confidence 0.09 Published 2009 Journal Endocrine, metabolic & immune disorders drug targets Section Abstract Doc Link 19594416 Disease Relevance 1.39 Pain Relevance 0.88
The fusion protein expressed from the chimeric tox gene was designated DT-(1-389)-LIF-(2-184)-peptide.
Gene_expression (expressed) of fusion protein
3) Confidence 0.05 Published 1996 Journal Eur. J. Biochem. Section Abstract Doc Link 8917449 Disease Relevance 0.57 Pain Relevance 0
PMP22 cDNA produced by the reverse transcriptase-polymerase chain reaction from rat sciatic nerve was expressed in Escherichia coli as a fusion protein with glutathione-S-transferase (GST).
Gene_expression (expressed) of fusion protein in sciatic nerve associated with sciatic nerve
4) Confidence 0.05 Published 1998 Journal Brain Section Abstract Doc Link 9798745 Disease Relevance 0.69 Pain Relevance 0.47
Furthermore, both AQP4 isoforms were cloned into the pcDNA3.1 Directional TOPO Expression vector (Invitrogen, Carlsbad, CA, USA), to express M-1 and M-23 AQP4 without the EmGFP fusion protein.
Gene_expression (express) of EmGFP fusion protein in M-1
5) Confidence 0.03 Published 2010 Journal PLoS ONE Section Body Doc Link PMC2864757 Disease Relevance 0.27 Pain Relevance 0.12
In addition to the DMARDs discussed above, there are nine biologic therapies approved for RA in the US18 and Europe.19 Etanercept is an IgG fusion protein produced through the recombinant soluble p75 receptor for tumor necrosis factor-alpha (TNF-?).
Gene_expression (produced) of IgG fusion protein associated with necrosis, cancer, rheumatoid arthritis and etanercept
6) Confidence 0.03 Published 2010 Journal Drug Design, Development and Therapy Section Body Doc Link PMC2990387 Disease Relevance 0.58 Pain Relevance 0.47
Fusion protein was not detectable on day 7 in both plasmid treated and NP treated groups, indicating the need for further optimization of the non-viral vector for prolonged retinal gene expression.
Neg (not) Gene_expression (detectable) of Fusion protein
7) Confidence 0.01 Published 2007 Journal Molecular Vision Section Body Doc Link PMC2768759 Disease Relevance 0 Pain Relevance 0
However, no fusion protein was detectable in animals treated with naked pSOD.
Neg (no) Gene_expression (detectable) of fusion protein
8) Confidence 0.01 Published 2007 Journal Molecular Vision Section Body Doc Link PMC2768759 Disease Relevance 0 Pain Relevance 0
Intravitreal injection of HSA NP to the mouse eye at a dose of 130 ng of plasmid produced detectable level of fusion protein expression at 48 h, compared to non-detectable expression in control animals.


Gene_expression (expression) of fusion protein in eye
9) Confidence 0.01 Published 2007 Journal Molecular Vision Section Abstract Doc Link PMC2768759 Disease Relevance 0 Pain Relevance 0
For the nuclear lamina disruption assays, U-2 OS cells grown on coverslips were co-transfected with expression plasmids for the indicated CHPK and pEGFPhLA-WT [72] that expresses a GFP-lamin A fusion protein (a kind gift of David Gilbert).
Gene_expression (expresses) of fusion protein in U-2 OS
10) Confidence 0.01 Published 2010 Journal PLoS Pathogens Section Body Doc Link PMC2936540 Disease Relevance 0.39 Pain Relevance 0
A tabulation of all reported CS cases with known mutations in CSB reveals that 21 of 24 retain at least one allele that should allow continued expression of the CSB-transposase fusion protein (Table S1).
Gene_expression (expression) of fusion protein associated with cockayne syndrome
11) Confidence 0.01 Published 2008 Journal PLoS Genetics Section Body Doc Link PMC2268245 Disease Relevance 0.40 Pain Relevance 0
Finally, we show that the CSB-transposase fusion protein continues to be expressed in CS primary cells lacking functional CSB protein, implying that the fusion protein could contribute to the CS phenotype, or even transform the mild UV sensitivity caused by complete loss of CSB-related proteins [33] into a true progeria.


Gene_expression (expressed) of fusion protein associated with hutchinson-gilford progeria syndrome and cockayne syndrome
12) Confidence 0.01 Published 2008 Journal PLoS Genetics Section Body Doc Link PMC2268245 Disease Relevance 0.34 Pain Relevance 0
The resulting CSB-transposase fusion protein is as abundant as CSB protein itself in a variety of human cell lines, and continues to be expressed by primary CS cells in which functional CSB is lost due to mutations beyond exon 5.
Gene_expression (expressed) of fusion protein associated with cockayne syndrome
13) Confidence 0.01 Published 2008 Journal PLoS Genetics Section Abstract Doc Link PMC2268245 Disease Relevance 0.55 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.
Gene_expression (expression) of fusion protein associated with targeted disruption and cockayne syndrome
14) Confidence 0.01 Published 2008 Journal PLoS Genetics Section Body Doc Link PMC2268245 Disease Relevance 0.94 Pain Relevance 0.08
Repression of PiggyBac and/or MER85 mobility may explain the initial domestication of PGBD3 more than 43 Mya, but the CSB-PGBD3 fusion protein continues to be conserved and abundantly expressed in primates despite the passage of sufficient time to inactivate existing PGBD-related transposases.
Gene_expression (expressed) of fusion protein associated with repression
15) Confidence 0.01 Published 2008 Journal PLoS Genetics Section Body Doc Link PMC2268245 Disease Relevance 0.16 Pain Relevance 0
Consistent with this hypothesis, 21 of the 24 molecularly characterized CS genotypes appear capable of expressing the CSB-PGBD3 fusion protein (Figure 7 and Table S1).
Gene_expression (expressing) of fusion protein associated with cockayne syndrome
16) Confidence 0.01 Published 2008 Journal PLoS Genetics Section Body Doc Link PMC2268245 Disease Relevance 0.86 Pain Relevance 0.06
To confirm that CS cells express the fusion protein in the absence of intact CSB, as seen for the hTERT-immortalized CS1AN line (Figure 3B), we screened three different primary CSB cells (GM10903, GM10905, and GM00739B derived from patient CS1AN) none of which, as expected, exhibited intact CSB protein.
Gene_expression (express) of fusion protein associated with cockayne syndrome
17) Confidence 0.01 Published 2008 Journal PLoS Genetics Section Body Doc Link PMC2268245 Disease Relevance 0.33 Pain Relevance 0
We have also confirmed experimentally that the fusion protein continues to be expressed in primary cells from 3 severely affected CS patients (Figure 5) including patient CS1AN whose CSB genotype is known (Table S1).
Gene_expression (expressed) of fusion protein associated with cockayne syndrome
18) Confidence 0.01 Published 2008 Journal PLoS Genetics Section Body Doc Link PMC2268245 Disease Relevance 0.85 Pain Relevance 0.05
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.
Gene_expression (expressed) of fusion protein associated with cockayne syndrome
19) Confidence 0.01 Published 2008 Journal PLoS Genetics Section Body Doc Link PMC2268245 Disease Relevance 0.28 Pain Relevance 0.11
The conserved CSB-PGBD3 fusion protein is expressed in both primary and established CS cells (Figures 2, 3, 5, and Figure S3), and could explain these mysteries if the fusion protein, which is advantageous in the presence of functional CSB (Tables 1 and 2), were detrimental in its absence.
Gene_expression (expressed) of fusion protein associated with cockayne syndrome
20) Confidence 0.01 Published 2008 Journal PLoS Genetics Section Body Doc Link PMC2268245 Disease Relevance 1.00 Pain Relevance 0.10

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