-
This study identifies the NEIL3 promoter possessing a G-rich element that can adopt a G4 fold, and when 8-oxo-7,8-dihydroguanine is incorporated, the sequence can lock into a more stable G4 fold via recruitment of the fifth track of Gs.
-
Results suggest a novel role for the DNA glycosylase Neil3 in atherogenesis in balancing lipid metabolism and macrophage function, potentially independently of genome-wide canonical base excision repair of oxidative DNA damage.
-
NEIL3 protects genome stability through targeted repair of oxidative damage in telomeres during S/G2 phase.
-
NEIL3-dependent modulation of DNA methylation regulates cardiac fibroblast proliferation and thereby affects extracellular matrix modulation after myocardial infarction.
-
Data indicate that DNA glycosylases MYH, UNG2, MPG, NTH1, NEIL1, 2 and 3 on nascent DNA.
-
These findings demonstrate that deficiency in NEIL3 is associated with increased lymphocyte apoptosis, autoantibodies, and predisposition to autoimmunity.
-
SNPs in NEIL3 are associated with impulsivity in Native American sample.
-
Single nucleotide polymorphism (SNP) rs142310826 near the NEIL3 gene showed a genome-wide significant interaction with caffeine consumption .There was no gender difference for this interaction (P = 0.64 for heterogeneity). NEIL3, a gene belonging to the base excision DNA repair pathway, encodes a DNA glycosylase that recognizes and removes lesions produced by oxidative stress.
-
The abnormal expressions of NEIL1, NEIL2, and NEIL3 are involved in cancer through their association with the somatic mutation load.
-
NEIL3 rs12645561 SNP TT genotype was associated with increased risk of myocardial infarction.
-
Polymorphisms within FLT3, EGFR, NEIL3, and ALOX5 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 is to repair DNA base damages in telomeres in vivo and that Neil3 and Neil1 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).
-
both the transcription and protein levels of hNEIL3 fluctuated during the cell cycle
-
NEIL3 partially rescues an E. coli nth nei mutant from hydrogen peroxide sensitivity. Taken together, repair of certain base damage including base loss in ssDNA may be mediated by NEIL3.
-
hFPG1 and hFPG2 repair 8-oxoguanine and other DNA oxidation products. (hFPG1 and hFPG2)
