about
Characterization of the human SNM1A and SNM1B/Apollo DNA repair exonucleasesThe Chemical Biology of Human Metallo-β-Lactamase Fold ProteinsA UV-induced genetic network links the RSC complex to nucleotide excision repair and shows dose-dependent rewiring.Components of a Fanconi-like pathway control Pso2-independent DNA interstrand crosslink repair in yeast.EXD2 promotes homologous recombination by facilitating DNA end resectionSunlight-induced mutagenicity of a common sunscreen ingredientMgm101: A double-duty Rad52-like protein.Human HEL308 localizes to damaged replication forks and unwinds lagging strand structuresOrchestrating the nucleases involved in DNA interstrand cross-link (ICL) repair.CSB interacts with SNM1A and promotes DNA interstrand crosslink processingStructural Basis of Metallo-β-Lactamase Inhibition by Captopril StereoisomersXPF protein levels determine sensitivity of malignant melanoma cells to oxaliplatin chemotherapy: suitability as a biomarker for patient selection.A small molecule inhibitor of the BLM helicase modulates chromosome stability in human cells.Repair of DNA interstrand crosslinks: molecular mechanisms and clinical relevance.Schizosaccharomyces pombe checkpoint response to DNA interstrand cross-linksRPA activates the XPF-ERCC1 endonuclease to initiate processing of DNA interstrand crosslinks.Small molecule inhibitors uncover synthetic genetic interactions of human flap endonuclease 1 (FEN1) with DNA damage response genes.DNA interstrand cross-link repair in Saccharomyces cerevisiae.The SNM1/Pso2 family of ICL repair nucleases: from yeast to man.DNA interstrand crosslink repair during G1 involves nucleotide excision repair and DNA polymerase zetaHuman SNM1A and XPF-ERCC1 collaborate to initiate DNA interstrand cross-link repair.A prosurvival DNA damage-induced cytoplasmic interferon response is mediated by end resection factors and is limited by Trex1.XPF-ERCC1 participates in the Fanconi anemia pathway of cross-link repair.Human SNM1A suppresses the DNA repair defects of yeast pso2 mutants.A FancD2-monoubiquitin fusion reveals hidden functions of Fanconi anemia core complex in DNA repair.Novel reagents for chemical cleavage at abasic sites and UV photoproducts in DNAA prototypical Fanconi anemia pathway in lower eukaryotes?Cephalosporins inhibit human metallo β-lactamase fold DNA repair nucleases SNM1A and SNM1B/apollo.Quantitative analysis of survivin protein expression and its therapeutic depletion by an antisense oligonucleotide in human lung tumors.The structures of the SNM1A and SNM1B/Apollo nuclease domains reveal a potential basis for their distinct DNA processing activities.DNA interstrand cross-link repair in the Saccharomyces cerevisiae cell cycle: overlapping roles for PSO2 (SNM1) with MutS factors and EXO1 during S phasePathways for Holliday junction processing during homologous recombination in Saccharomyces cerevisiae.DNA sequence selective adenine alkylation, mechanism of adduct repair, and in vivo antitumor activity of the novel achiral seco-amino-cyclopropylbenz[e]indolone analogue of duocarmycin AS-I-145.In Silico Fragment-Based Design Identifies Subfamily B1 Metallo-β-lactamase Inhibitors.Tumor survivin is downregulated by the antisense oligonucleotide LY2181308: a proof-of-concept, first-in-human dose studyCharacterization of DNA damage inflicted by free radicals from a mutagenic sunscreen ingredient and its location using an in vitro genetic reversion assayAlteration in the choice of DNA repair pathway with increasing sequence selective DNA alkylation in the minor groovePCR-based methods for detecting DNA damage and its repair at the sub-gene and single nucleotide levels in cellsApollo: a healer of the genome?XPF-ERCC1: Linchpin of DNA crosslink repair
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description
researcher
@en
wetenschapper
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հետազոտող
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name
Peter J McHugh
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Peter J McHugh
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Peter J McHugh
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Peter J McHugh
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Peter J McHugh
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type
label
Peter J McHugh
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Peter J McHugh
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Peter J McHugh
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Peter J McHugh
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Peter J McHugh
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Peter J McHugh
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Peter J McHugh
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Peter J McHugh
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Peter J McHugh
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Peter J McHugh
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P106
P21
P31
P496
0000-0002-8679-4627