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Nonetheless, using a highly MSH2 (zeige MSH2 Proteine)-dependent mechanism, Ung (zeige UNG Proteine)(-/-) Smug1(-/-) mice can still produce detectable levels of switched isotypes, especially IgG1
SMUG1 is the dominant glycosylase responsible for 5-hydroxymethyluracil-excision in mice as well as the major UNG (zeige UNG Proteine)-backup for U-excision.
analysis of species specific differences between mouse and humans in regulation of SMUG1 and UNG2 (zeige UNG Proteine)
The structure and specificity of SMUG1 have been solved.
A case-control study of 801 bladder cancer patients and 801 matched controls, the associations of 167 single nucleotide polymorphisms (SNPs) from 19 genes of the BER pathway with the risk of bladder cancer; 13 SNPs in 10 Base excision repair (BER) pathway genes were significantly associated with bladder cancer risk; most significant SNP was rs2029167 in the SMUG1 gene.
Single-strand selective monofunctional uracil-DNA glycosylase (SMUG1) deficiency is linked to aggressive breast cancer and predicts response to adjuvant therapy.
The results obtained suggest the potential role of the g.4235T>C and the c.-31A>G polymorphisms in AMD (zeige AMD1 Proteine) pathogenesis.
There was no difference between SMUG1 proficient and depleted cells following continuous exposure.
SMUG1 is a DKC1 (zeige DKC1 Proteine) interaction partner that contributes to rRNA quality control, partly by regulating 5-hydroxymethyluridine levels.
Data show that uracil-DNA glycosylases SMUG1 and UNG2 (zeige CCNO Proteine) display widely different sequence preferences.
there was increased risk of breast cancer among postmenopausal women heterozygous for either SMUG1 rs2029166 or rs7296239. Among premenopausal women, the increased risk associated with SMUG1 rs2029166 was limited to those with low folate intake.
analysis of species specific differences between mouse and humans in regulation of SMUG1 and UNG2 (zeige CCNO Proteine)
SMUG1 plays little natural role in antibody diversification.
This gene encodes a protein that participates in base excision repair by removing uracil from single- and double-stranded DNA. Many alternatively spliced transcript variants exist for this gene\; the full-length nature is known for some but not all of the variants.
single-strand-selective monofunctional uracil-DNA glycosylase 1
, single-strand selective monofunctional uracil DNA glycosylase
, single-strand selective monofunctional uracil-DNA glycosylase