Results 51 to 60 of about 678 (148)

Structure of Formamidopyrimidine-DNA Glycosylase Covalently Complexed to DNA [PDF]

open access: yesJournal of Biological Chemistry, 2002
Formamidopyrimidine-DNA glycosylase (Fpg) is a DNA repair enzyme that excises oxidized purines from damaged DNA. The Schiff base intermediate formed during this reaction between Escherichia coli Fpg and DNA was trapped by reduction with sodium borohydride, and the structure of the resulting covalently cross-linked complex was determined at a 2.1-A ...
Rotem, Gilboa   +8 more
openaire   +2 more sources

Uracil Accumulation and Mutagenesis Dominated by Cytosine Deamination in CpG Dinucleotides in Mice Lacking UNG and SMUG1

open access: yesScientific Reports, 2017
Both a DNA lesion and an intermediate for antibody maturation, uracil is primarily processed by base excision repair (BER), either initiated by uracil-DNA glycosylase (UNG) or by single-strand selective monofunctional uracil DNA glycosylase (SMUG1).
Lene Alsøe   +15 more
doaj   +1 more source

Bacillus Calmette-Guerin Increases Base Excision Repair in Bladder Cancer Cells

open access: yesJournal of Urological Surgery, 2021
Objective:Most patients with non-muscle-invasive bladder cancer (NMIBC) do not respond to intravesical Bacillus Calmette-Guerin (BCG) immunotherapy and have high risk of NMIBC recurrence and progression.
Selçuk Keskin   +2 more
doaj   +1 more source

Genome‐wide network analysis identifies the lncRNA‐92467/miR‐205‐5p/PTPRM/CAMs axis in a rat model of hypoxic pulmonary hypertension

open access: yesAnimal Models and Experimental Medicine, EarlyView.
The pathogenesis of hypoxic pulmonary hypertension (HPH) remains unclear. In this study, we explored its key regulatory mechanisms using animal models, RNA sequencing, and cellular assays. We found that lncRNA‐92467 functions as a ceRNA, binding miR‐205‐5p, and thereby upregulating PTPRM, inhibiting abnormal proliferation and migration of endothelial ...
Yan‐Ying Shen   +7 more
wiley   +1 more source

A ratiometric electrochemical assay for human 8-oxoguanine DNA glycosylase amplified by hybridization chain reaction

open access: yesElectrochemistry Communications, 2019
Human 8-oxoguanine DNA glycosylase 1 (hOGG1) is an important DNA repair enzyme, which is closely related to the occurrence and development of certain diseases.
Dawei Yang   +3 more
doaj   +1 more source

Bridging the Gap Between Human Toxicology and Ecotoxicology Under One Health Perspective by a Cross‐Species Adverse Outcome Pathway Network for Reproductive Toxicity

open access: yesEnvironmental Toxicology and Chemistry, EarlyView.
Cross‐species extrapolation of adverse outcome pathway network on reproductive toxicity under the One Health perspective using new approach methodologies. AOP = adverse outcome pathway. Abstract Although ecotoxicological and toxicological risk assessments are performed separately from each other, recent efforts have been made in both disciplines to ...
Elizabeth Dufourcq Sekatcheff   +2 more
wiley   +1 more source

Uracil-DNA glycosylase as a probe for protein-DNA interactions [PDF]

open access: yesNucleic Acids Research, 1993
The DNA repair enzyme Uracil-DNA Glycosylase (UDG) can be used to investigate three different features of protein-DNA interactions. Complexes can be probed by simple protection experiments ('footprinting') or by two kinds of interference assays: a missing thymine site (MT-site) experiment and a missing thymine methyl site (MTM-site) experiment.
P R, Devchand   +2 more
openaire   +2 more sources

PERFUME: detection of 8-oxoguanine DNA glycosylase activity based on primer exchange reaction and functionalized hemin/G-quadruplex DNAzyme

open access: yesTalanta Open
Background: 8-oxoguanine DNA glycosylase can maintain genomic stability and integrity. However, it can interfere with the regular DNA damage repair process, possibly leading to the development of cancer and various other human diseases when its activity ...
Kaiting Xiao   +8 more
doaj   +1 more source

Uracil in DNA and its processing by different DNA glycosylases [PDF]

open access: yesPhilosophical Transactions of the Royal Society B: Biological Sciences, 2008
Uracil in DNA may result from incorporation of dUMP during replication and from spontaneous or enzymatic deamination of cytosine, resulting in U:A pairs or U:G mismatches, respectively. Uracil generated by activation-induced cytosine deaminase (AID) in B cells is a normal intermediate in adaptive immunity. Five mammalian uracil-DNA
Torkild, Visnes   +9 more
openaire   +2 more sources

Structure of a DNA Glycosylase Bound to a Nicked T:G Mismatch-Containing DNA

open access: yesMolecules
Mismatched T:G base pairs can arise during de novo replication as well as base excision repair (BER). In particular, the action of the gap-filling polymerase β (Polβ) can generate a T:G pair as well as a nick in the DNA backbone.
Hala Ouzon-Shubeita   +3 more
doaj   +1 more source

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