Browse our N-Methylpurine-DNA Glycosylase Proteins (MPG)

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N-Methylpurine-DNA Glycosylase Proteins (MPG)
On are 13 N-Methylpurine-DNA Glycosylase (MPG) Proteins from 6 different suppliers available. Additionally we are shipping N-Methylpurine-DNA Glycosylase Antibodies (107) and N-Methylpurine-DNA Glycosylase Kits (7) and many more products for this protein. A total of 135 N-Methylpurine-DNA Glycosylase products are currently listed.
9830006D05, Aag, ADPG, AI326268, anpg, APNG, BA3871, CRA36.1, MDG, Mid1, MPG, MPGR, PIG11, PIG16, si:xx-187g17.9, zgc:162984
list all proteins Gene Name GeneID UniProt
MPG 4350 P29372
MPG 268395 Q04841
MPG 24561  

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N-Methylpurine-DNA Glycosylase Proteins (MPG) by Origin

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Top referenced N-Methylpurine-DNA Glycosylase Proteins

  1. Human MPG Protein expressed in Escherichia coli (E. coli) - ABIN667935 : Adhikari, Uren, Roy: Excised damaged base determines the turnover of human N-methylpurine-DNA glycosylase. in DNA repair 2009 (PubMed)
    Show all 2 references for 667935

More Proteins for N-Methylpurine-DNA Glycosylase Interaction Partners

Human N-Methylpurine-DNA Glycosylase (MPG) interaction partners

  1. Rheumatoid arthritis is associated with a polymorphism in the MPG gene (rs2858056) and increased serum level of the MPG protein.

  2. Role of MPG protein in the DNA damage response through the base excision repair pathway

  3. results suggest that individuals carrying R120C and R141Q MPG variants may be at risk for genomic instability and associated diseases as a consequence.

  4. Elevated MPG activity is associated with lung cancer, possibly by creating an imbalance in the base excision repair pathway.

  5. High MPG DNA repair assays for two different oxidative DNA lesions reveal associations with increased lung cancer risk.

  6. disease-stage-specific alterations in the expression of MPG may highlight a potential role for MPG in determining EAC (show CYLD Proteins) onset and thus potentially be of clinical relevance for early disease detection and increased patient survival.

  7. 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

  8. 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.

  9. Mitochondrial single-stranded binding protein (mtSSB (show SSBP1 Proteins)) as a novel interacting partner of AAG.

  10. UHRF1 (show UHRF1 Proteins) interacts with N-methylpurine DNA glycosylase (MPG) in cancer cells in vitro and displays a co-localization with MPG in the nucleoplasm.

Mouse (Murine) N-Methylpurine-DNA Glycosylase (MPG) interaction partners

  1. The depletion of Aag (show C16orf35 Proteins) did not significantly change the transcriptional inhibitory or mutagenic properties of all five examined lesions, suggesting a negligible role of Aag (show C16orf35 Proteins) in the repair of these DNA adducts in mammalian cells.

  2. 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 Proteins), but not AAG (show C16orf35 Proteins), as a key node in determining a carcinogenic threshold.

  3. the detrimental effects of Aag (show C16orf35 Proteins)-initiated BER during I/R and sterile inflammation, and present a novel target for controlling I/R-induced injury.

  4. Toxicity, induced by tert (show TERT Proteins)-butyl-hydroperoxide and potassium bromate, differs in base excision repair proficient (Mpg (+/+), Nth1 (+/+)) and deficient (Mpg (-/-), Nth1 (-/-)) mouse embryonic fibroblasts following Msh2 (show MSH2 Proteins) knockdown, was examined.

  5. These results provide in vivo evidence that Aag (show C16orf35 Proteins)-initiated BER may play a critical role in determining the side-effects of alkylating agent chemotherapies and that Parp1 (show PARP1 Proteins) plays a crucial role in Aag (show C16orf35 Proteins)-mediated tissue damage.

  6. ALKBH2 (show ALKBH2 Proteins) and ALKBH3 (show ALKBH3 Proteins) provide cancer protection similar to that of the DNA glycosylase AAG (show C16orf35 Proteins) and display apparent epistasis with Aag (show C16orf35 Proteins)

  7. AAG (show C16orf35 Proteins) is a mammalian enzyme that can act on all three purine deamination bases, hypoxanthine, xanthine, and oxanine

  8. 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

  9. Aag (show C16orf35 Proteins)-mediated DNA repair prevents colonic epithelial damage and reduces the severity of dextran sulfate sodium-induced colon tumorigenesis.

  10. Aag (show C16orf35 Proteins)-initiated base excision repair drives alkylation-induced retinal degeneration.

N-Methylpurine-DNA Glycosylase (MPG) Protein Profile

Protein Summary

enzyme that cleaves 3-methyladenine and 7-methylguanine residues from DNA

Alternative names and synonyms associated with N-Methylpurine-DNA Glycosylase (MPG)

  • DNA-3-methyladenine glycosidase (alkA)
  • DNA-3-methyladenine glycosidase (CNL04530)
  • DNA-3-methyladenine glycosidase (cgd8_5410)
  • DNA-3-methyladenine glycosidase (Xfasm12_0684)
  • N-methylpurine-DNA glycosylase (MPG)
  • N-methylpurine-DNA glycosylase (mpg)
  • si:xx-by187g17.9 (si:xx-by187g17.9)
  • N-methylpurine-DNA glycosylase (CpB0526)
  • N-methylpurine-DNA glycosylase (gll2491)
  • N-methylpurine-DNA glycosylase (Mpg)
  • 9830006D05 protein
  • Aag protein
  • ADPG protein
  • AI326268 protein
  • anpg protein
  • APNG protein
  • BA3871 protein
  • CRA36.1 protein
  • MDG protein
  • Mid1 protein
  • MPG protein
  • MPGR protein
  • PIG11 protein
  • PIG16 protein
  • si:xx-187g17.9 protein
  • zgc:162984 protein

Protein level used designations for MPG

DNA-3-methyladenine glycosidase , N-methylpurine-DNA glycosylase , DNA-3-methyladenine glycosylase , 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) , N-methylpurine-DNA glycosylase, MPG , proliferation-inducing protein 11 , proliferation-inducing protein 16 , 3-methyladenine DNA glycosylase , ADPG , alkylpurine-DNA-N-glycosylase , N-methylpurine-DNA glycocylase

1088762 Bacillus anthracis str. Ames
1796118 Rhodopirellula baltica SH 1
3255007 Cryptococcus neoformans var. neoformans JEC21
3374666 Cryptosporidium parvum Iowa II
6119369 Xylella fastidiosa M12
416648 Gallus gallus
566516 Danio rerio
571211 Danio rerio
618306 Bos taurus
749794 Pan troglodytes
1467205 Chlamydophila pneumoniae TW-183
2600892 Gloeobacter violaceus PCC 7421
100579173 Sus scrofa
4350 Homo sapiens
611597 Canis lupus familiaris
268395 Mus musculus
24561 Rattus norvegicus
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