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NEIL3-dependent modulation of DNA methylation (zeige HELLS Proteine) regulates cardiac fibroblast proliferation and thereby affects extracellular matrix modulation after myocardial infarction.
Data indicate that DNA glycosylases MYH (zeige MUTYH Proteine), UNG2 (zeige CCNO Proteine), MPG (zeige MPG Proteine), NTH1, NEIL1 (zeige NEIL1 Proteine), 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 (zeige NEIL1 Proteine), NEIL2 (zeige NEIL2 Proteine), 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 (zeige FLT3 Proteine), EGFR (zeige EGFR Proteine), NEIL3, and ALOX5 (zeige ALOX5 Proteine) 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 (zeige NEIL1 Proteine) is to repair DNA base damages in telomeres in vivo and that Neil3 and Neil1 (zeige NEIL1 Proteine) may function in quadruplex-mediated cellular events, such as gene regulation via removal of damaged bases from quadruplex DNA.
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.
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 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 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