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Human Polyclonal MPG Primary Antibody for ICC, IF - ABIN4335346
Ström, Johansson, Uhlén, Szigyarto, Erixon, Helleday: Poly (ADP-ribose) polymerase (PARP) is not involved in base excision repair but PARP inhibition traps a single-strand intermediate. in Nucleic acids research 2011
Show all 2 Pubmed References
Human Monoclonal MPG Primary Antibody for IF, IHC (p) - ABIN561837
Chou, Wang, Wong, Ding, Wu, Shieh, Shen: Chk2-dependent phosphorylation of XRCC1 in the DNA damage response promotes base excision repair. in The EMBO journal 2008
Human Polyclonal MPG Primary Antibody for ELISA, WB - ABIN268629
Samson, Derfler, Boosalis, Call: Cloning and characterization of a 3-methyladenine DNA glycosylase cDNA from human cells whose gene maps to chromosome 16. in Proceedings of the National Academy of Sciences of the United States of America 1991
PIG11 may act as a candidate liver tumor suppressor.
high levels of APNG were associated with better overall survival in patients with glioblastoma
Data indicate that DNA glycosylases MYH, UNG2, MPG, NTH1, NEIL1, 2 and 3 on nascent DNA.
Data suggest that the change in tryptophan fluorescence of Y162W mutant of AAG (alkyladenine DNA glycosylase) is extremely rapid upon binding to either damaged or undamaged DNA, much faster than lesion-recognition and nucleotide flipping steps; thus, intercalation by tyrosine may be one of the earliest steps in search for/recognition of DNA damage.
Rheumatoid arthritis is associated with a polymorphism in the MPG gene (rs2858056) and increased serum level of the MPG protein.
Role of MPG protein in the DNA damage response through the base excision repair pathway
results suggest that individuals carrying R120C and R141Q MPG variants may be at risk for genomic instability and associated diseases as a consequence.
Elevated MPG activity is associated with lung cancer, possibly by creating an imbalance in the base excision repair pathway.
In the case of alkyladenine DNA glycosylase, DNA intercalation contributes to the specific binding of a damaged nucleotide, but this enhanced specificity comes at the cost of reduced speed of nucleotide flipping.
High MPG DNA repair assays for two different oxidative DNA lesions reveal associations with increased lung cancer risk.
disease-stage-specific alterations in the expression of MPG may highlight a potential role for MPG in determining EAC onset and thus potentially be of clinical relevance for early disease detection and increased patient survival.
AAG has a flexible amino terminus that tunes its affinity for nonspecific DNA, but we find that it is not required for intersegmental transfer. As AAG has only a single DNA binding site, this argues against the bridging model for intersegmental transfer
AAG removes both methanol and 1,N(6)-ethenoadenine from DNA with single-turnover rate constants that are significantly greater than the corresponding uncatalyzed rates.
Mitochondrial single-stranded binding protein (mtSSB) as a novel interacting partner of AAG.
UHRF1 interacts with N-methylpurine DNA glycosylase (MPG) in cancer cells in vitro and displays a co-localization with MPG in the nucleoplasm.
A functional footprinting approach was used to define the binding site of alkyladenine DNA glycosylase used for the repair of deaminated purines.
N-methylpurine DNA glycosylase negatively regulates p53-mediated cell cycle arrest.
AAG can make damaged DNA by catalyzing formation of an N-glycosyl bond between 1,N(6)-ethenoadenine (epsilonA) and abasic DNA. We attribute the reversibility of this reaction to the tight binding and slow subsequent hydrolysis of DNA containing an epsilonA lesion.
Investigated the expression of MPG gene and protein in 128 glioma and 10 non-neoplastic brain tissues. Found MPG gene expression level in glioma tissues was significantly higher than that in non-neoplastic brain tissues (P < 0.001).
The non-enzymatic binding of AAG to 3,N(4)-ethenocytosine specifically blocks ALKBH2-catalyzed repair of 3,N(4)-ethenocytosine but not that of methylated ALKBH2 substrates.
The depletion of Aag did not significantly change the transcriptional inhibitory or mutagenic properties of all five examined lesions, suggesting a negligible role of Aag in the repair of these DNA adducts in mammalian cells.
This study demonstrates for the first time a non-linear dose-response for alkylation-induced colorectal carcinogenesis and reveals DNA repair by MGMT, but not AAG, as a key node in determining a carcinogenic threshold.
the detrimental effects of Aag-initiated BER during I/R and sterile inflammation, and present a novel target for controlling I/R-induced injury.
Toxicity, induced by tert-butyl-hydroperoxide and potassium bromate, differs in base excision repair proficient (Mpg (+/+), Nth1 (+/+)) and deficient (Mpg (-/-), Nth1 (-/-)) mouse embryonic fibroblasts following Msh2 knockdown, was examined.
These results provide in vivo evidence that Aag-initiated BER may play a critical role in determining the side-effects of alkylating agent chemotherapies and that Parp1 plays a crucial role in Aag-mediated tissue damage.
ALKBH2 and ALKBH3 provide cancer protection similar to that of the DNA glycosylase AAG and display apparent epistasis with Aag
AAG is a mammalian enzyme that can act on all three purine deamination bases, hypoxanthine, xanthine, and oxanine
the N-terminal tail in MPG plays a critical role in overcoming product inhibition, which is achieved by reducing the differences of MPG binding affinity toward hypoxanthine and apurinic/apyrimidinic sites
Aag-mediated DNA repair prevents colonic epithelial damage and reduces the severity of dextran sulfate sodium-induced colon tumorigenesis.
Aag-initiated base excision repair drives alkylation-induced retinal degeneration.
Clock gene mutation modulates the cellular sensitivity to genotoxic stress through altering the expression of Mpg gene.
RNS-induced posttranslational modification of AAG is one mechanism of base excision repair dysregulation
enzyme that cleaves 3-methyladenine and 7-methylguanine residues from DNA
3' end of the Mid1 gene, localized 68 kb upstream the humanzeta globin gene on 16p
, 3-alkyladenine DNA glycosylase
, 3-methyladenine DNA glycosidase
, CRA36.1 (3-methyl-adenine DNA glycosylase)
, DNA-3-methyladenine glycosylase
, N-methylpurine-DNA glycosylase, MPG
, proliferation-inducing protein 11
, proliferation-inducing protein 16
, N-methylpurine-DNA glycocylase
, 3-methyladenine DNA glycosylase
, N-methylpurine-DNA glycosylase