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Toxicity, induced by tert (show TERT Antibodies)-butyl-hydroperoxide and potassium bromate, differs in base excision repair proficient (Mpg (show MPG Antibodies) (+/+), Nth1 (+/+)) and deficient (Mpg (show MPG Antibodies) (-/-), Nth1 (-/-)) mouse embryonic fibroblasts following Msh2 (show MSH2 Antibodies) knockdown, was examined.
These results suggest that Nth1 plays an important role in telomere maintenance and base repair against oxidative stress-induced (show SQSTM1 Antibodies) base modifications.
deficiencies in Ogg1 (show OGG1 Antibodies) and/or Nth1 do not lead to decreased DNA double strand breaks
To determine the significance of thymine glycol repair in mammals, a mouse model with mutated mNth1, a homolog of nth (show APEX1 Antibodies), was made by gene targeting. Mutant mouse liver, instead of mNTH1 activity, had at least 2 novel DNA glycosylase activities against Tg.
To determine the role of murine Nth1 in protecting genomic integrity, a knockout strain was created. No phenotypic changes from wild type were noted due to a novel AP endonuclease DNA repair system.
NEIL1 (show NEIL1 Antibodies) is a back-up glycosylase for NTH1 with unique substrate specificity and tissue-specific expression
ability of nth1 to discriminate between thymine glycol stereoisomers
results indicated that 8-oxoguanine DNA-glycosylase (OGG1 (show OGG1 Antibodies)) and nth (endonuclease III)-like 1(NTH1) are the major DNA glycosylases for the removal of 2,6-diamino-4-hydroxy-5-formamidopyrimidine (FapyG) and 4,6-diamino-5-formamidopyrimidine (FapyA)
The high incidence of tumors in Nth1-/-Neil1 (show NEIL1 Antibodies)-/- mice together with the activating mutation in the K-ras (show HRAS Antibodies) gene of their pulmonary tumors, reveal for the first time, the existence of mutagenic and carcinogenic oxidative damage to DNA which is not 8-OH-Gua (show DDX21 Antibodies).
Data indicate that DNA glycosylases MYH (show MUTYH Antibodies), UNG2 (show CCNO Antibodies), MPG (show MPG Antibodies), NTH1, NEIL1 (show NEIL1 Antibodies), 2 and 3 on nascent DNA.
WT NTHL1 (human) and Nth (show APEX1 Antibodies) (E. coli) are remarkably alike with respect to specificity of glycosylase reaction, and although NTHL1 is a much slower enzyme than Nth (show APEX1 Antibodies), the tighter binding of NTHL1 compensates, resulting in similar kcat/Kd values for both enzymes with each of the substrates tested. For NTHL1 Gln287Ala, specificity for substrates positioned opposite G is lost, but not that of substrates positioned opposite A.
We therefore found published evidence to support the association between variants in NTHL1 and RPS20 (show RPS20 Antibodies) with CRC (show CALR Antibodies).
Both Ntg1 and its human homologue, NTHL1, can be SUMO-modified in response to oxidative stress.
NTH1 polymorphisms may be associated with non-small cell lung cancer pathogenesis.
This study extends the description of biallelic mutations in NTHL1 beyond the single c.268C-->T,p.Q90* mutation that was observed previously.
A homozygous loss-of-function germline mutation in the NTHL1 gene predisposes to a new subtype of BER-associated adenomatous polyposis and colorectal cancer.
NTH1 is involved in removal of 8-oxoguanine from 8-oxoguanine/guanine mispairs in DNA
substrate selectivity of mammalian NTH1 and the concomitant selective stimulation of activity by APE1 (show APEX1 Antibodies) are indicative of selective repair of oxidative damage in different regions of the genome
search for the factors interacting with NTH1 shows GST (show SLCO6A1 Antibodies)-NTH1 fusion protein precipitates proliferating cell nuclear antigen (PCNA (show PCNA Antibodies)) and p53 (show TP53 Antibodies) as well as XPG (show ERCC5 Antibodies) from human cell-free extracts
The protein encoded by this gene is a DNA N-glycosylase of the endonuclease III family. Like a similar protein in E. coli, the encoded protein has DNA glycosylase activity on DNA substrates containing oxidized pyrimidine residues and has apurinic/apyrimidinic lyase activity.
endonuclease III-like protein 1
, thymine glycol DNA glycosylase/AP lyase
, nth endonuclease III-like 1