INT182413

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Context Info
Confidence 0.46
First Reported 2005
Last Reported 2010
Negated 1
Speculated 2
Reported most in Body
Documents 17
Total Number 21
Disease Relevance 2.44
Pain Relevance 0.22

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

nucleoplasm (OGG1) mitochondrion (OGG1) lyase activity (OGG1)
hydrolase activity, acting on glycosyl bonds (OGG1) nucleolus (OGG1) nucleus (OGG1)
OGG1 (Homo sapiens)
OGG1 - S326C (2)
Pain Link Frequency Relevance Heat
imagery 17 75.84 Quite High
Glutamate 16 70.88 Quite High
Pain 17 8.44 Low Low
ischemia 9 5.00 Very Low Very Low Very Low
Inflammation 9 5.00 Very Low Very Low Very Low
alcohol 4 5.00 Very Low Very Low Very Low
cINOD 3 5.00 Very Low Very Low Very Low
Inflammatory response 3 5.00 Very Low Very Low Very Low
Crohn's disease 3 5.00 Very Low Very Low Very Low
cerebral cortex 1 5.00 Very Low Very Low Very Low
Disease Link Frequency Relevance Heat
Genomic Instability 3 99.92 Very High Very High Very High
Myeloid Leukemia 7 99.80 Very High Very High Very High
Nasopharynx Cancer 103 97.76 Very High Very High Very High
Cancer 210 92.44 High High
Cockayne Syndrome 32 86.56 High High
Stress 78 83.28 Quite High
Angiomyolipoma 12 80.36 Quite High
Inflammatory Bowel Disease 21 79.60 Quite High
Nicotine Addiction 2 77.68 Quite High
Renal Disease 1 61.44 Quite High

Sentences Mentioned In

Key: Protein Mutation Event Anatomy Negation Speculation Pain term Disease term
Interestingly, the anti-phosphoserine recognized a phosphorylated form of the enzyme in both EGFP-hOGG1 and EGFP-hOGG1-Glu326 chromatin fractions.


EGFP-hOGG1 Binding (recognized) of
1) Confidence 0.46 Published 2005 Journal Nucleic Acids Research Section Body Doc Link PMC1072800 Disease Relevance 0 Pain Relevance 0.06
We have previously shown that hOGG1 is associated with the soluble chromatin and the nuclear matrix during interphase and with condensed chromatin during mitosis (47).
hOGG1 Binding (associated) of
2) Confidence 0.40 Published 2005 Journal Nucleic Acids Research Section Body Doc Link PMC1072800 Disease Relevance 0 Pain Relevance 0
As EGFP-hOGG1 has been shown to be associated with the soluble chromatin and the nuclear matrix during interphase (47), we wanted to investigate whether these associations were maintained for the EGFP-hOGG1-Cys326 mutant protein.
EGFP-hOGG1 Binding (associated) of
3) Confidence 0.40 Published 2005 Journal Nucleic Acids Research Section Body Doc Link PMC1072800 Disease Relevance 0 Pain Relevance 0
By sequentially extracting the cells to obtain cytoplasm, soluble chromatin and the nuclear matrix, we were able to show that EGFP-hOGG1-Glu326 was associated with both the soluble chromatin and the nuclear matrix fractions (Figure 7D, lanes 2 and 4).
EGFP-hOGG1 Binding (associated) of
4) Confidence 0.34 Published 2005 Journal Nucleic Acids Research Section Body Doc Link PMC1072800 Disease Relevance 0 Pain Relevance 0.06
Within the next 2 h, cells enter the M-phase, the nuclear envelope disassembles and EGFP-hOGG1 associates with chromatin (Figure 4).
EGFP-hOGG1 Binding (associates) of
5) Confidence 0.34 Published 2005 Journal Nucleic Acids Research Section Body Doc Link PMC1072800 Disease Relevance 0 Pain Relevance 0
The pEYFP-hOGG1 plasmid was constructed by ligating the hOGG1 cDNA fragment from pEGFP-hOGG1 into the pEYFP-N1 vector.
hOGG1 Binding (ligating) of
6) Confidence 0.31 Published 2005 Journal Nucleic Acids Research Section Body Doc Link PMC1072800 Disease Relevance 0 Pain Relevance 0
As neither a functional nor a physical direct interaction was detected between these two proteins, the authors hypothesize a protein complex containing among others CSB and hOGG1.
hOGG1 Neg (neither) Binding (interaction) of
7) Confidence 0.31 Published 2005 Journal Nucleic Acids Research Section Body Doc Link PMC1072800 Disease Relevance 0.17 Pain Relevance 0
The pEYFP-hOGG1 plasmid was constructed by ligating the hOGG1 cDNA fragment from pEGFP-hOGG1 into the pEYFP-N1 vector.
hOGG1 Binding (ligating) of
8) Confidence 0.31 Published 2005 Journal Nucleic Acids Research Section Body Doc Link PMC1072800 Disease Relevance 0 Pain Relevance 0
As shown in Figure 2B, EGFP-hOGG1 is associated with the nucleoli during S-phase.
EGFP-hOGG1 Binding (associated) of
9) Confidence 0.31 Published 2005 Journal Nucleic Acids Research Section Body Doc Link PMC1072800 Disease Relevance 0 Pain Relevance 0
Interestingly, the anti-phosphoserine recognized a phosphorylated form of the enzyme in both EGFP-hOGG1 and EGFP-hOGG1-Glu326 chromatin fractions.


EGFP-hOGG1 Binding (recognized) of
10) Confidence 0.31 Published 2005 Journal Nucleic Acids Research Section Body Doc Link PMC1072800 Disease Relevance 0 Pain Relevance 0.06
Thus, the nucleolus might be a sequestering compartment of hOGG1 to avoid the accumulation of GC?
hOGG1 Spec (might) Binding (compartment) of
11) Confidence 0.31 Published 2005 Journal Nucleic Acids Research Section Body Doc Link PMC1072800 Disease Relevance 0 Pain Relevance 0
Finally, we wanted to examine whether EGFP-hOGG1-Glu326 would also be associated with the soluble chromatin and the nuclear matrix.
EGFP-hOGG1 Binding (associated) of
12) Confidence 0.30 Published 2005 Journal Nucleic Acids Research Section Body Doc Link PMC1072800 Disease Relevance 0 Pain Relevance 0.04
Finally, by mimicking a hOGG1 protein phosphorylated at Ser-326 we demonstrate that the regulation of the nucleolar localization, soluble chromatin, nuclear matrix and condensed chromatin association of hOGG1 are mediated through the phosphorylation of Ser-326.


hOGG1 Binding (association) of
13) Confidence 0.30 Published 2005 Journal Nucleic Acids Research Section Body Doc Link PMC1072800 Disease Relevance 0 Pain Relevance 0
EGFP (30 kDa), EGFP-hOGG1, EGFP-hOGG1-Cys326 and EGFP-hOGG1-Glu326 (68 kDa) were recognized by the anti-GFP specific antibody (Figure 3A) while only EGFP-hOGG1, EGFP-hOGG1-Cys326 and EGFP-hOGG1-Glu326 (68 kDa) were recognized by the anti-OGG1 specific antibody (Figure 3B).
EGFP-hOGG1 Binding (recognized) of
14) Confidence 0.30 Published 2005 Journal Nucleic Acids Research Section Body Doc Link PMC1072800 Disease Relevance 0 Pain Relevance 0
Thus, compartmentalization of hOGG1 to the nucleoli during S-phase might increase the repair efficiency of A:8-oxoG mispairs that arise during DNA replication, as dCMP or dAMP can be selectively incorporated opposite 8-oxoG (7).
hOGG1 Spec (might) Binding (compartmentalization) of
15) Confidence 0.30 Published 2005 Journal Nucleic Acids Research Section Body Doc Link PMC1072800 Disease Relevance 0 Pain Relevance 0
Thus, we suggest that the Ser-326 has to be phosphorylated to interact with a protein during S-phase that will translocate EGFP-hOGG1 to the nucleolus and to the condensed chromosomes during mitosis.
EGFP-hOGG1 Binding (interact) of
16) Confidence 0.30 Published 2005 Journal Nucleic Acids Research Section Body Doc Link PMC1072800 Disease Relevance 0.08 Pain Relevance 0
In humans, 8-oxodG is repaired by 8-oxoguanine DNA glycosylase (OGG1), an enzyme that recognizes and hydrolyzes the aberrant base from the DNA backbone.
OGG1 Binding (recognizes) of
17) Confidence 0.28 Published 2010 Journal PLoS ONE Section Body Doc Link PMC2910735 Disease Relevance 0.10 Pain Relevance 0
OGG1 is the DNA repair enzyme that recognizes and excises 8-oxodG [70].
OGG1 Binding (recognizes) of
18) Confidence 0.28 Published 2010 Journal PLoS ONE Section Body Doc Link PMC2910735 Disease Relevance 0.32 Pain Relevance 0
In humans, 8-oxodG is repaired by 8-oxoguanine DNA glycosylase (OGG1), an enzyme that recognizes and hydrolyzes the aberrant base from the DNA backbone.
DNA glycosylase Binding (recognizes) of
19) Confidence 0.24 Published 2010 Journal PLoS ONE Section Body Doc Link PMC2910735 Disease Relevance 0.11 Pain Relevance 0
They identified showed the presence of significant association between the Ser326Cys polymorphism of OGG1 and AML.
OGG1 (S326C) Binding (association) of associated with myeloid leukemia
20) Confidence 0.24 Published 2008 Journal Current Genomics Section Body Doc Link PMC2691673 Disease Relevance 0.83 Pain Relevance 0

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