scispace - formally typeset
T

Thomas E. Spratt

Researcher at Pennsylvania State University

Publications -  68
Citations -  1927

Thomas E. Spratt is an academic researcher from Pennsylvania State University. The author has contributed to research in topics: DNA polymerase & DNA. The author has an hindex of 26, co-authored 66 publications receiving 1801 citations. Previous affiliations of Thomas E. Spratt include Ohio State University & Penn State Cancer Institute.

Papers
More filters
Journal ArticleDOI

Interaction of Sirt3 with OGG1 contributes to repair of mitochondrial DNA and protects from apoptotic cell death under oxidative stress

TL;DR: A new function and mechanism is revealed for Sirt3 in defending the mitochondrial genome against oxidative damage and protecting from the genotoxic stress-induced apoptotic cell death but also provides evidence supporting a new mtDNA repair pathway.
Journal ArticleDOI

Evidence for 4-(3-pyridyl)-4-oxobutylation of DNA in F344 rats treated with the tobacco-specific nitrosamines 4-(methylnitrosamino)-1-(3-pyridyl)-1-butanone and N'-nitrosonornicotine.

TL;DR: Results demonstrate that 4-(3-pyridyl)-4-oxobutylation of DNA occurs in rats treated with NNK or NNN, and are consistent with the hypothesis that these nitrosamines are metabolically activated by alpha-hydroxylation.
Journal ArticleDOI

Pyridyloxobutyl adduct O6-[4-oxo-4-(3-pyridyl)butyl]guanine is present in 4-(acetoxymethylnitrosamino)-1-(3-pyridyl)-1-butanone-treated DNA and is a substrate for O6-alkylguanine-DNA alkyltransferase.

TL;DR: O6-pobG was removed, presumably a result of transfer of the pyridyloxobutyl group from the O6-position of guanine to AGT's active site, when [5-3H]NNKOAc-treated DNA was incubated with either rat liver or recombinant human AGT.
Journal ArticleDOI

An unprecedented nucleic acid capture mechanism for excision of DNA damage

TL;DR: Crystal structures of the recently discovered Bacillus cereus AlkD glycosylase in complex with DNAs containing alkylated, mismatched and abasic nucleotides are presented, providing an illustration for how hydrolysis of N3- and N7-alkylated bases may be facilitated by increased lifetime out of the DNA helix.
Journal ArticleDOI

Glucuronidation of tobacco-specific nitrosamines by UGT2B10.

TL;DR: UGT2B10 is likely the most active UGT isoform in human liver for the N-glucuronidation of TSNAs, and real-time polymerase chain reaction analysis showed that it was expressed at a level that was 26% higher than that observed for UGT1A4 in a screening of normal liver tissue specimens from 20 individual subjects.