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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 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
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
high levels of APNG were associated with better overall survival in patients with glioblastoma
Data indicate that DNA glycosylases MYH (show MUTYH Antibodies), UNG2 (show CCNO Antibodies), MPG, NTH1, NEIL1 (show NEIL1 Antibodies), 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.
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 (show CYLD Antibodies) 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
The depletion of Aag (show C16orf35 Antibodies) did not significantly change the transcriptional inhibitory or mutagenic properties of all five examined lesions, suggesting a negligible role of Aag (show C16orf35 Antibodies) 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 (show MGMT Antibodies), but not AAG (show C16orf35 Antibodies), as a key node in determining a carcinogenic threshold.
the detrimental effects of Aag (show C16orf35 Antibodies)-initiated BER during I/R and sterile inflammation, and present a novel target for controlling I/R-induced injury.
Toxicity, induced by tert (show TERT Antibodies)-butyl-hydroperoxide and potassium bromate, differs in base excision repair proficient (Mpg (+/+), Nth1 (+/+)) and deficient (Mpg (-/-), Nth1 (-/-)) mouse embryonic fibroblasts following Msh2 (show MSH2 Antibodies) knockdown, was examined.
These results provide in vivo evidence that Aag (show C16orf35 Antibodies)-initiated BER may play a critical role in determining the side-effects of alkylating agent chemotherapies and that Parp1 (show PARP1 Antibodies) plays a crucial role in Aag (show C16orf35 Antibodies)-mediated tissue damage.
ALKBH2 (show ALKBH2 Antibodies) and ALKBH3 (show ALKBH3 Antibodies) provide cancer protection similar to that of the DNA glycosylase AAG (show C16orf35 Antibodies) and display apparent epistasis with Aag (show C16orf35 Antibodies)
AAG (show C16orf35 Antibodies) 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 (show C16orf35 Antibodies)-mediated DNA repair prevents colonic epithelial damage and reduces the severity of dextran sulfate sodium-induced colon tumorigenesis.
Aag (show C16orf35 Antibodies)-initiated base excision repair drives alkylation-induced retinal degeneration.
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