Results 41 to 50 of about 24,501 (233)

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

Phylogenomic Analysis of the Uracil-DNA Glycosylase Superfamily [PDF]

open access: yesMolecular Biology and Evolution, 2010
The spontaneous deamination of cytosine produces uracil mispaired with guanine in DNA, which will produce a mutation, unless repaired. In all domains of life, uracil-DNA glycosylases (UDGs) are responsible for the elimination of uracil from DNA.
J Ignacio, Lucas-Lledó   +2 more
openaire   +2 more sources

Life without dUTPase

open access: yesFrontiers in Microbiology, 2016
Fine-tuned regulation of the cellular nucleotide pools is indispensable for faithful replication of DNA. The genetic information is also safeguarded by DNA damage recognition and repair processes.
Csaba Kerepesi   +9 more
doaj   +1 more source

Uracil-DNA glycosylase. Purification and properties of uracil-DNA glycosylase from Micrococcus luteus.

open access: yesJournal of Biological Chemistry, 1982
A uracil-DNA-glycosylase from Micrococcus luteus has been purified more than 3,000-fold. The enzyme preparation appears homogeneous, according to the results of sodium dodecyl sulfate-polyacrylamide gel electrophoresis. It is devoid of nonspecific endonucleases, specific endonucleases for apurinic and apyrimidinic sites, 3-methyladenine or 7 ...
J P, Leblanc   +3 more
openaire   +2 more sources

Secondary Structure of Uracil-DNA Glycosylase Inhibitor Protein [PDF]

open access: yesJournal of Biological Chemistry, 1995
The Bacillus subtilis bacteriophage PBS2 uracil-DNA glycosylase inhibitor (Ugi) is an acidic protein of 84 amino acids that inactivates uracil-DNA glycosylase from diverse organisms (Wang, Z., and Mosbaugh, D. W. (1989) J. Biol. Chem. 264, 1163-1171). The secondary structure of Ugi has been determined by solution state multidimensional nuclear magnetic
S, Balasubramanian   +4 more
openaire   +2 more sources

Terminal Deoxynucleotidyl Transferase and T7 Exonuclease-Aided Amplification Strategy for Ultrasensitive Detection of Uracil-DNA Glycosylase.

open access: yesAnalytical Chemistry, 2018
As one of the key initiators of the base excision repair process, uracil-DNA glycosylase (UDG) plays an important role in maintaining genomic integrity. It has been found that aberrant expression of UDG is associated with a variety of diseases.
Yichen Du   +7 more
semanticscholar   +1 more source

Uracil-DNA glycosylase activities in hyperthermophilic micro-organisms [PDF]

open access: yesFEMS Microbiology Letters, 1996
Hyperthermophiles exist in conditions which present an increased threat to the informational integrity of their DNA, particularly by hydrolytic damage. As in mesophilic organisms, specific activities must exist to restore and protect this template function of DNA.
A, Koulis   +3 more
openaire   +2 more sources

Real-time PCR method for detection of short DNA using a deoxyuridine probe and application for detection of fomivirsen

open access: yesBioTechniques, 2022
This study sought to develop a short DNA detection method using a deoxyuridine probe and polymerase chain reaction. The probe was hybridized to the target short DNA, which was then extended by DNA polymerase.
Naoki Harikai   +4 more
doaj   +1 more source

Onset of deaminase APOBEC3B induction in response to DNA double-strand breaks

open access: yesBiochemistry and Biophysics Reports, 2018
Deamination of 5-methyl cytosine is a major cause of cancer-driver mutations in inflammation-associated cancers. The deaminase APOBEC3B is expressed in these cancers and causes mutations under replication stress; however, the mechanisms by which APOBEC3B
Atsuhiro Shimizu   +6 more
doaj   +1 more source

Tertiary Structure of Uracil-DNA Glycosylase Inhibitor Protein [PDF]

open access: yesJournal of Biological Chemistry, 1995
The Bacillus subtilis bacteriophage PBS2 uracil-DNA glycosylase inhibitor (Ugi) is an acidic protein of 84 amino acids that inactivates uracil-DNA glycosylase from diverse organisms. The secondary structure of Ugi consists of five anti-parallel beta-strands and two alpha-helices (Balasubramanian, S., Beger, R.D., Bennett, S.E., Mosbaugh, D.W., and ...
R D, Beger   +4 more
openaire   +2 more sources

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