• Publications
  • Influence
Biological consequences of free radical-damaged DNA bases.
  • S. Wallace
  • Biology
    Free radical biology & medicine
  • 1 July 2002
Abortive base-excision repair of radiation-induced clustered DNA lesions in Escherichia coli
TLDR
It is shown that clustered DNA damages are indeed formed in Escherichia coli by ionizing radiation and are converted to lethal double-strand breaks during attempted base-excision repair.
Nucleosome Disruption by DNA Ligase III-XRCC1 Promotes Efficient Base Excision Repair
TLDR
Findings provide insights into rate-limiting steps that govern BER in chromatin and reveal a unique role for ligase IIIα-XRCC1 in enhancing the efficiency of the final two steps in the BER of lesions in nucleosomes.
Escherichia coli endonuclease VIII: cloning, sequencing, and overexpression of the nei structural gene and characterization of nei and nei nth mutants
TLDR
Double mutants lacking both endonucleases III and VIII exhibited a strong spontaneous mutator phenotype as determined by a rifampin forward mutation assay, and nei single mutants behaved as the wild type.
The crystal structure of human endonuclease VIII-like 1 (NEIL1) reveals a zincless finger motif required for glycosylase activity.
TLDR
The crystal structure of a human Nei-like (NEIL) enzyme, NEIL1, revealed that it contains a structural motif composed of two antiparallel beta-strands that mimics the antipar parallel beta-hairpin zinc finger found in other Fpg/Nei family members but lacks the loops that harbor the zinc-binding residues and, therefore, does not coordinate zinc.
The mouse ortholog of NEIL3 is a functional DNA glycosylase in vitro and in vivo
TLDR
The characterization of Mus musculus (house mouse) Neil3 (MmuNeil3) as an active DNA glycosylase both in vitro and in vivo is reported, suggesting that Neil3 plays a role in repairing FapyG in vivo.
Saccharomyces cerevisiae Ntg1p and Ntg2p: broad specificity N-glycosylases for the repair of oxidative DNA damage in the nucleus and mitochondria.
TLDR
The results expand the known substrate specificities of Ntg1p and Ntg2p, indicating that their base damage recognition ranges show distinct differences and that these proteins mediate different roles in the repair of DNA base damage in the nucleus and mitochondria of yeast.
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