Results 211 to 220 of about 2,038,987 (238)
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Structural Biology of the HEAT‐Like Repeat Family of DNA Glycosylases
Bioessays, 2018DNA glycosylases remove aberrant DNA nucleobases as the first enzymatic step of the base excision repair (BER) pathway. The alkyl‐DNA glycosylases AlkC and AlkD adopt a unique structure based on α‐helical HEAT repeats.
R. Shi +3 more
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DNA glycosylase recognition and catalysis
Current Opinion in Structural Biology, 2004DNA 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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Processivity of uracil DNA glycosylase
Mutation Research/DNA Repair, 1993The 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 Glycosylases in DNA Repair
1986The 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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Uracil-DNA Glycosylases and DNA Uracil Repair
1989Publisher 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 N-glycosylases and UV repair
Nature, 1980Repair 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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Structures and functions of DNA glycosylases
Mutation Research/DNA Repair, 1990Treatment of cells with a methylating agent, such as methyl methanesulfonate (MMS) and Nmethyl-N-nitrosourea (MNU), yields various methylated bases in DNA (Riazuddin and Lindahl, 1978). Organisms possess mechanisms to repair these methylated bases, which are potentially harmful to their genetic material.
K, Sakumi, M, Sekiguchi
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Novel DNA glycosylases from Mycobacterium tuberculosis
Biochemistry (Moscow), 2008Oxidized bases are removed from DNA of Escherichia coli by enzymes formamidopyrimidine DNA glycosylase (Eco-Fpg) and endonuclease VIII (Eco-Nei) of the same structural family Fpg/Nei. New homologs of these enzymes not characterized earlier have been found in genomes of Actinobacteria.
V S, Sidorenko +4 more
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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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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, 1983Urea-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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