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NEIL1 and NEIL2 (show NEIL2 ELISA Kits) cooperate with TDG (show TDG ELISA Kits) during base excision: TDG (show TDG ELISA Kits) occupies the abasic site and is displaced by NEILs, which further process the baseless sugar, thereby stimulating TDG (show TDG ELISA Kits)-substrate turnover.
Findings suggesting that DNA glycosylase NEIL1 c.C844T is a defective allele.
NEIL1 forms a multiprotein complex with DNA replication proteins via its C-terminal domain, allowing recruitment at the replication fork.
Results show that YB-1 (show YBX1 ELISA Kits) interferes negatively with the AP site DNA cleavage activity of both APE1 (show APEX1 ELISA Kits) and NEIL1 for ssDNA and bubble structures.
Rad9 (show RAD9A ELISA Kits) regulates base excision repair by controlling NEIL1 transcription.
genome and cancer single nucleotide polymorphisms of the human NEIL1 DNA glycosylase
The NEIL1 rs4462560 SNP may serve as a predictor of acute RIET and RP risk but not of overall survival.
one role for Neil3 (show NEIL3 ELISA Kits) and NEIL1 is to repair DNA base damages in telomeres in vivo and that Neil3 (show NEIL3 ELISA Kits) and Neil1 may function in quadruplex-mediated cellular events, such as gene regulation via removal of damaged bases from quadruplex DNA.
Prereplicative repair of oxidized bases in the human genome is mediated by NEIL1 DNA glycosylase together with replication proteins.
Authors show that the intrinsically disordered C-terminal domain interacts with the folded domain in native NEIL1 containing 389 residues.
Rad9 (show RAD9A ELISA Kits) regulates base excision repair by controlling Neil1 protein stability in mouse embryonic stem cells.
Hypersensitivity to H2O2 caused by NEIL1 knockdown was more significant in S phase than in G1 phase, suggesting that NEIL1 has an important role during S phase.
Data indicate that maternal folate depletion during pregnancy and high-fat feeding from weaning altered gene expression of Ogg1 (show OGG1 ELISA Kits), Neil1, Mutyh (show MUTYH ELISA Kits) and Xrcc1 (show XRCC1 ELISA Kits) in the brain of adult offspring.
binds to the BRCT domain of PARP-1 (show PARP1 ELISA Kits)
Neil1 contributes to germline and somatic Huntington's disease CAG repeat (show CELF3 ELISA Kits) expansion.
Endonuclease VIII-like 1 (NEIL1) promotes short-term spatial memory retention and protects from ischemic stroke-induced brain dysfunction and death in mice.
NEIL1 deficiency results in an increased susceptibility to obesity and related complications potentially by lowering the threshold for tolerance of cellular oxidative stress in neil1(-/-) mice.
NEIL1 is involved in nucleotide excision repair of(5'R)- and (5'S)-8,5'-cyclo-2'-deoxyadenosines, in addition to its function as a DNA glycosylase in base excision repair.
NEIL1 is a back-up glycosylase for NTH1 (show NTHL1 ELISA Kits) with unique substrate specificity and tissue-specific expression.
This gene is a member of the Nei endonuclease VIII-like gene family which encodes DNA glycosylases. The encoded enzyme participates in the DNA repair pathway by initiating base excision repair by removing damaged bases, primarily oxidized pyrimidines. Multiple transcript variants encoding different isoforms have been found for this gene.
endonuclease VIII-like 1
, DNA glycosylase/AP lyase Neil1
, DNA-(apurinic or apyrimidinic site) lyase Neil1
, endonuclease 8-like 1
, endonuclease VIII
, nei homolog 1
, nei-like protein 1