Results 141 to 150 of about 7,033 (174)
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Processivity of uracil DNA glycosylase

Mutation Research/DNA Repair, 1993
The purpose of this study was to determine the mechanism by which uracil DNA glycosylase locates uracil residues within double-stranded DNA. Using reaction conditions that contained low salt concentrations, the addition of uracil DNA glycosylase to plasmid DNAs containing multiple, randomly incorporated uracils resulted in the accumulation of form III ...
M, Higley, R S, Lloyd
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DNA glycosylase recognition and catalysis

Current Opinion in Structural Biology, 2004
DNA glycosylases are the enzymes responsible for recognizing base lesions in the genome and initiating base excision DNA repair. Recent structural and biochemical results have provided novel insights into DNA damage recognition and repair. The basis of the recognition of the oxidative lesion 8-oxoguanine by two structurally unrelated DNA glycosylases ...
J Christopher, Fromme   +2 more
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Thymine DNA glycosylase

2001
More than 50% of colon cancer-associated mutations in the p53 tumor suppressor gene are C-->T transitions. The majority of them locate in CpG dinucleotides and are thought to have arisen through spontaneous hydrolytic deamination of 5-methylcytosine. This deamination process gives rise to G.T mispairs that need to be repaired to G.C in order to avoid C-
Hardeland, U.   +5 more
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A new class of uracil-DNA glycosylases related to human thymine-DNA glycosylase

Nature, 1996
Mispairs in DNA of guanine with uracil and thymine can arise as a result of deamination of cytosine and 5-methylcytosine, respectively. In humans such mispairs are removed by thymine-DNA glycosylase (TDG). By deleting the carboxy and amino termini of this enzyme we have identified a core region capable of processing G/U but not G/T mispairs.
Gallinari, P, Jiricny, J
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Uracil-DNA Glycosylases and DNA Uracil Repair

1989
Publisher Summary This chapter reviews the DNA uracil repair and uracil–DNA glycosylases (UDG). The major source of DNA uracil in prokaryotic and eukaryotic cells is transient incorporation of dUMP during replication. This replicative uracil is quickly repaired by UDG, apyramidinic/apurinic (AP) endonucleases, and other enzymes of excision repair ...
N V, Tomilin, O N, Aprelikova
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DNA Glycosylases in DNA Repair

1986
The excision of potentially mutagenic and lethal lesions from DNA proceeds by one of two different routes. DNA damage which results in a major distortion of the DNA double-helix is generally recognized by a high-molecular weight nuclease that cuts two phosphodiester bonds in the altered strand, one on each side of the lesion.
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DNA N-glycosylases and UV repair

Nature, 1980
Repair of some DNA photoproducts can be mediated by glycosylic bond hydrolysis. Thus, Escherichia coli endonuclease III releases 5,6-hydrated thymines as free bases, while T4 UV endonuclease releases one of two glycosylic bonds holding pyrimidine dimers in DNA. In contrast, uninfected E.
B, Demple, S, Linn
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Induction of the DNA repair enzymes uracil DNA glycosylase and 3-methyladenine DNA glycosylase in regenerating rat liver

Carcinogenesis, 1981
The capacity of eukaryotic cells to modulate the activities of DNA repair enzymes during cell proliferation was examined. Using regenerating rat liver as a model system, the specific activities of the DNA repair enzymes uracil DNA glycosylase and 3-methyladenine DNA glycosylase were determined at specific intervals after partial hepatectomy.
C T, Gombar   +3 more
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27 DNA Glycosylases

1981
Publisher Summary DNA glycosylases are ubiquitous in nature and essentially hydrolyze nucleoside base–glycosidic bonds. The reaction results in the production of an apurinic/apyrimidinic (AP) site in DNA and a free nucleoside base. These enzymes also participate in DNA repair processes by catalyzing the removal of unconventional or damaged bases from
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Urea-DNA glycosylase in mammalian cells

Biochemistry, 1983
Urea-DNA glycosylase, an enzyme presumed to be active in the repair of DNA damage caused by oxidizing agents, has been identified previously in Escherichia coli. This enzyme has now been shown to be present in cell extracts of calf thymus and human fibroblasts.
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