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NEIL3 rs12645561 SNP TT genotype was associated with increased risk of myocardial infarction.
Polymorphisms within FLT3 (show FLT3 Proteins), EGFR (show EGFR Proteins), NEIL3, and ALOX5 (show ALOX5 Proteins) may contribute to the occurrence of GBM.
Results show that the base excision and strand incision activities of NEIL3 exhibited a non-concerted action, indicating that NEIL3 mainly operates as a monofunctional DNA glycosylase.
one role for Neil3 and NEIL1 (show NEIL1 Proteins) is to repair DNA base damages in telomeres in vivo and that Neil3 and Neil1 (show NEIL1 Proteins) may function in quadruplex-mediated cellular events, such as gene regulation via removal of damaged bases from quadruplex DNA.
Here we report the construction of bicistronic expression vectors for expressing in Escherichia coli the full-length mouse Neil3 (MmuNeil3), its glycosylase domain (MmuNeil3Delta324), as well as the glycosylase domain of human Neil3 (NEIL3Delta324).
NEIL3 partially rescues an E. coli nth (show APEX1 Proteins) nei (show PMCH Proteins) mutant from hydrogen peroxide sensitivity. Taken together, repair of certain base damage including base loss in ssDNA may be mediated by NEIL3.
hFPG1 (show NEIL1 Proteins) and hFPG2 repair 8-oxoguanine and other DNA oxidation products. (hFPG1 (show NEIL1 Proteins) and hFPG2)
Structural insight into the substrate specificity and marked preference of Neil3 for ssDNA.
Our data support the involvement of Neil3 in removal of replication blocks in proliferating cells.
Neil3-dependent repair of oxidative DNA damage in neural stem/progenitor cells is required for maintenance of adult neurogenesis to counteract the age-associated deterioration of cognitive performance.
Neil3 exercises a highly specialized function through accurate molecular repair of DNA in rapidly proliferating cells
Neil3 plays a role in repairing 2,6-diamino-4-hydroxy-5-formamidopyrimidine in vivo.
NEIL3 is localized in the nuclei; Neil3 mRNA was selectively expressed in thymus, spleen and bone marrow
NEIL3 is specifically expressed in brain areas where neurogenesis takes place during development and that its expression is tightly regulated both temporally and spatially. NEIL3 seems to be upregulated in tumor tissues compared to normal tissues.
NEIL3 belongs to a class of DNA glycosylases homologous to the bacterial Fpg/Nei family. These glycosylases initiate the first step in base excision repair by cleaving bases damaged by reactive oxygen species and introducing a DNA strand break via the associated lyase reaction (Bandaru et al., 2002
endonuclease VIII-like 3
, nei like 3
, nei endonuclease VIII-like 3 (E. coli)
, nei endonuclease VIII-like 3
, DNA glycosylase FPG2
, DNA glycosylase hFPG2
, DNA glycosylase/AP lyase Neil3
, endonuclease 8-like 3
, nei-like protein 3