Search Results - "Nitiss, Karin C"
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Genome Instability Induced by Topoisomerase Misfunction
Published in International journal of molecular sciences (24-09-2024)“…Topoisomerases alter DNA topology by making transient DNA strand breaks (DSBs) in DNA. The DNA cleavage reaction mechanism includes the formation of a…”
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Aberrant topoisomerase-1 DNA lesions are pathogenic in neurodegenerative genome instability syndromes
Published in Nature neuroscience (01-06-2014)“…In this study, the authors show that topoisomerase-1–DNA cleavage complex (Top1cc) accumulation may be involved in the onset of ataxia telangiectasia and…”
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Proteolytic Degradation of Topoisomerase II (Top2) Enables the Processing of Top2·DNA and Top2·RNA Covalent Complexes by Tyrosyl-DNA-Phosphodiesterase 2 (TDP2)
Published in The Journal of biological chemistry (27-06-2014)“…Eukaryotic type II topoisomerases (Top2α and Top2β) are homodimeric enzymes; they are essential for altering DNA topology by the formation of normally…”
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TDP1 is required for efficient non-homologous end joining in human cells
Published in DNA repair (01-12-2017)“…•Loss of TDP1 significantly reduces end joining of restriction enzyme induced DSBs in human cells.•TDP1-deficeint human cells also show reduced end-joining…”
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Requirements for MRN endonuclease processing of topoisomerase II-mediated DNA damage in mammalian cells
Published in Frontiers in molecular biosciences (23-09-2022)“…During a normal topoisomerase II (TOP2) reaction, the enzyme forms a covalent enzyme DNA intermediate consisting of a 5′ phosphotyrosyl linkage between the…”
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TDP1 promotes assembly of non-homologous end joining protein complexes on DNA
Published in DNA repair (01-06-2015)“…•End-processing factor TDP1 interacts with the NHEJ factor XLF to form a TDP1:XLF:DNA complex.•XLF stimulates TDP1 enzymatic activity on dsDNA.•TDP1 also…”
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Tyrosyl-DNA Phosphodiesterase (Tdp1) Participates in the Repair of Top2-Mediated DNA Damage
Published in Proceedings of the National Academy of Sciences - PNAS (13-06-2006)“…Agents targeting topoisomerases are active against a wide range of human tumors. Stabilization of covalent complexes, converting topoisomerases into…”
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Tdp2: a means to fixing the ends
Published in PLoS genetics (01-03-2013)“… A key finding from the original identification of Tdp2 was that the protein was more active in processing 5' phosphotyrosyl-linked oligonucleotides, and that…”
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Yeast Tdp1 regulates the fidelity of nonhomologous end joining
Published in Proceedings of the National Academy of Sciences - PNAS (02-03-2010)“…Tyrosyl-DNA-phosphodiesterase 1 (Tdp1) can disjoin peptides covalently bound to DNA. We assessed the role of Tdp1 in nonhomologous end joining (NHEJ) and found…”
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Roles of nonhomologous end-joining pathways in surviving topoisomerase II–mediated DNA damage
Published in Molecular cancer therapeutics (01-06-2006)“…Topoisomerase II is a target for clinically active anticancer drugs. Drugs targeting these enzymes act by preventing the religation of enzyme-DNA covalent…”
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Enhancing drug accumulation in Saccharomyces cerevisiae by repression of pleiotropic drug resistance genes with chimeric transcription repressors
Published in Molecular pharmacology (01-08-2008)“…Yeast is a powerful model system for studying the action of small-molecule therapeutics. An important limitation has been low efficacy of many small molecules…”
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Modeling allosteric mechanisms of eukaryotic type II topoisomerases
Published in Biophysical journal (18-06-2024)“…Type II topoisomerases (TopoIIs) are ubiquitous enzymes that are involved in crucial nuclear processes such as genome organization, chromosome segregation, and…”
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Twisting and ironing: doxorubicin cardiotoxicity by mitochondrial DNA damage
Published in Clinical cancer research (15-09-2014)“…Anthracyclines are active clinical agents that have multiple mechanisms of cytotoxicity. Cardiotoxicity by anthracyclines limits the therapeutic potential of…”
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Recurrent mutations in topoisomerase IIα cause a previously undescribed mutator phenotype in human cancers
Published in Proceedings of the National Academy of Sciences - PNAS (25-01-2022)“…Topoisomerases nick and reseal DNA to relieve torsional stress associated with transcription and replication and to resolve structures such as knots and…”
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UnTTrapping the ends: A new player in overcoming protein linked DNA damage
Published in Cell research (01-02-2010)“…DNA topoisomerases carry out their reactions by generating transient covalent phosphotyrosine intermediates with DNA [ 1 ]. This reaction mechanism allows…”
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Using energy to go downhill—a genoprotective role for ATPase activity in DNA topoisomerase II
Published in Nucleic acids research (09-02-2024)“…Abstract Type II topoisomerases effect topological changes in DNA by cutting a single duplex, passing a second duplex through the break, and resealing the…”
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A conserved SUMO pathway repairs topoisomerase DNA-protein cross-links by engaging ubiquitin-mediated proteasomal degradation
Published in Science advances (13-11-2020)“…Topoisomerases form transient covalent DNA cleavage complexes to perform their reactions. Topoisomerase I cleavage complexes (TOP1ccs) are trapped by…”
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Naturally mutagenic sequence diversity in a human type II topoisomerase
Published in Proceedings of the National Academy of Sciences - PNAS (11-07-2023)“…Type II topoisomerases transiently cleave duplex DNA as part of a strand passage mechanism that helps control chromosomal organization and superstructure…”
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Trapped topoisomerase II initiates formation of de novo duplications via the nonhomologous end-joining pathway in yeast
Published in Proceedings of the National Academy of Sciences - PNAS (27-10-2020)“…Topoisomerase II (Top2) is an essential enzyme that resolves catenanes between sister chromatids as well as supercoils associated with the over- or…”
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Detection of Topoisomerase Covalent Complexes in Eukaryotic Cells
Published in Methods in molecular biology (Clifton, N.J.) (2018)“…DNA topoisomerases carry out topological transformations of DNA by introducing transient DNA breaks. The covalent intermediate of topoisomerase reactions…”
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