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NEIL1 and homotetrameric mtSSB form a larger ternary complex in presence of DNA, however, the tetrameric form of mtSSB gets disrupted by NEIL1 in the absence of DNA as revealed by the formation of a smaller NEIL1-mtSSBmonomer complex.
The major role of acetylable Lys residues in NEIL1 is to stabilize the formation of chromatin-bound repair complexes which protect cells from oxidative stress.
The level of OGG1 expression was significantly reduced in bipolar patients compared to healthy individuals, whereas the two groups exhibited similar levels of NEIL1 expression.
Data indicate that DNA glycosylases MYH, UNG2, MPG, NTH1, NEIL1, 2 and 3 on nascent DNA.
identified the c-Jun N-terminal kinase 1 (JNK1) as the kinase involved in the phosphorylation of NEIL1
NEIL1 (rs5745908) is associated with Behcet's disease. The genetic association in NEIL1 is a predicted splice donor variant that may introduce a deleterious intron retention and result in a noncoding transcript variant.
cellular NEIL1 is regulated by the UPP mediated by the E3 ubiquitin ligases Mule and TRIM26, which plays a vital role in co-ordinating the cellular response to DNA damage.
Nei Like DNA Glycosylase 1 (NEIL1) as a likely candidate gene due to its crucial role in B-cell activation and terminal differentiation.
The abnormal expressions of NEIL1, NEIL2, and NEIL3 are involved in cancer through their association with the somatic mutation load.
NEIL1 and NEIL2 cooperate with TDG during base excision: TDG occupies the abasic site and is displaced by NEILs, which further process the baseless sugar, thereby stimulating TDG-substrate turnover.
first study to show that SNPs of genes involved in DNA repair, may modulate the risk of Depressive Disorder.
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 interferes negatively with the AP site DNA cleavage activity of both APE1 and NEIL1 for ssDNA and bubble structures.
Rad9 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 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.
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.
Loss of Neil1 expression is associated with hepatocellular carcinoma.
Collectively the data suggest that NEIL1-initiated repair of a subset of ROS-induced DNA base lesions may be insufficient to prevent the initiation of inflammatory pathways during chronic UV exposure in mouse skin.
Its loss causes defects in olfactory function.
Rad9 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, Neil1, Mutyh and Xrcc1 in the brain of adult offspring.
binds to the BRCT domain of PARP-1
Neil1 contributes to germline and somatic Huntington's disease CAG repeat expansion.
Endonuclease VIII-like 1 (NEIL1) promotes short-term spatial memory retention and protects from ischemic stroke-induced brain dysfunction and death in mice.
These results suggest that mNEIL1 mRNA variants are expressed in a variety of organs in normal mice and that variant 1 protein may regulate mNEIL1 activity.
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 with unique substrate specificity and tissue-specific expression.
repression of Neil1 espression by RNA interference
Neil1 is an essential component of base excision repair in mammalian cells; its presence may contribute to the redundant repair capacity observed in Ogg1 -/- and Nth1 -/- mice
ability of Neil1 to discriminate between thymine glycol stereoisomers
NEIL1 and NEIL2 are essential in the recognition of oxidized lesions arising from 8-oxoG and may play important roles in the repair of DNA damage induced by carcinogenic metals.
Measurement of excision kinetics showed that mNEIL1 possesses equal specificity for 2,6-diamino-4-hydroxy-5-formamidopyrimidine and 4,6-diamino-5-formamidopyrimidine.
identified nei endonuclease VIII-like 1(NEIL1) in liver mitochondria, which could account for the residual DNA repair activity in the absence of OGG1 and NTH1
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