+ |
NFYA | up-regulates quantity by expression
transcriptional regulation
|
OGG1 |
0.268 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-254817 |
|
|
Homo sapiens |
|
pmid |
sentence |
14688259 |
these results demonstrate that MMS can up-regulate hOGG1 expression through the induction of the transcription factor, NF-YA, and increased transcription level of the hOGG1 gene correlates with an increase in enzyme activity providing functional protection from MMS. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
OGG1 | up-regulates
|
DNA_repair |
0.7 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-263959 |
|
|
Mus musculus |
|
pmid |
sentence |
26221032 |
Cut repeats from the CUX1 protein were recently shown to stimulate 8-oxoguanine DNA glycosylase 1 (OGG1), an enzyme that removes oxidized purines from DNA and introduces a single strand break through its apurinic/apyrimidinic lyase activity to initiate base excision repair. |
|
Publications: |
1 |
Organism: |
Mus Musculus |
+ |
TP53 | up-regulates quantity by expression
transcriptional regulation
|
OGG1 |
0.441 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-255440 |
|
|
Homo sapiens |
|
pmid |
sentence |
16293709 |
Using gel-shift assays, we showed that p53 binds to its putative cis-elements within the hOGG1 promoter. In addition we demonstrated that supplementing p53 in HCT116p53-/- cells enhanced the transcription of hOGG1. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
CUX2 | up-regulates activity
binding
|
OGG1 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-263960 |
|
|
Mus musculus |
|
pmid |
sentence |
26221032 |
CUX2 Interacts Directly with OGG1 and Stimulate Its Binding to DNA Containing 8-OxoG |
|
Publications: |
1 |
Organism: |
Mus Musculus |
+ |
OGG1 | up-regulates
|
Base-excision_repair |
0.7 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-275715 |
|
|
|
|
pmid |
sentence |
23545420 |
The BER pathway is initiated by one of at least 11 distinct DNA glycosylases, depending on the type of lesion (Table 1). |
|
Publications: |
1 |