Processing of nucleopeptides mimicking the topoisomerase I-DNA covalent complex by tyrosyl-DNA phosphodiesterase - Wikidata - wikimedia - TriplyDB

Processing of nucleopeptides mimicking the topoisomerase I-DNA covalent complex by tyrosyl-DNA phosphodiesterase

Processing of nucleopeptides mimicking the topoisomerase I-DNA covalent complex by tyrosyl-DNA phosphodiesterase

http://www.wikidata.org/entity/Q33584109

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Substrate specificity of tyrosyl-DNA phosphodiesterase I (Tdp1)Novel high-throughput electrochemiluminescent assay for identification of human tyrosyl-DNA phosphodiesterase (Tdp1) inhibitors and characterization of furamidine (NSC 305831) as an inhibitor of Tdp1 Diels-Alder cycloadditions in water for the straightforward preparation of peptide-oligonucleotide conjugates Drugging topoisomerases: lessons and challenges Mitochondrial DNA damage and its consequences for mitochondrial gene expression Solution structure and stability of tryptophan-containing nucleopeptide duplexes Tyrosyl-DNA phosphodiesterase (Tdp1) participates in the repair of Top2-mediated DNA damage Mutation of TDP1, encoding a topoisomerase I-dependent DNA damage repair enzyme, in spinocerebellar ataxia with axonal neuropathy TDP1 overexpression in human cells counteracts DNA damage mediated by topoisomerases I and II DNA Topoisomerase I Inhibitors: Chemistry, Biology, and Interfacial Inhibition Design and synthesis of fluorescent substrates for human tyrosyl-DNA phosphodiesterase I.Repair of DNA-polypeptide crosslinks by human excision nuclease.Identification of phosphotyrosine mimetic inhibitors of human tyrosyl-DNA phosphodiesterase I by a novel AlphaScreen high-throughput assay Suicidal cross-linking of PARP-1 to AP site intermediates in cells undergoing base excision repair.Role of tyrosyl-DNA phosphodiesterase (TDP1) in mitochondria.The DNA binding and 3'-end preferential activity of human tyrosyl-DNA phosphodiesterase.SUMO-targeted ubiquitin ligase, Rad60, and Nse2 SUMO ligase suppress spontaneous Top1-mediated DNA damage and genome instability.Tyrosyl-DNA-phosphodiesterases (TDP1 and TDP2).Pol β associated complex and base excision repair factors in mouse fibroblasts.Human Tdp1 cleaves a broad spectrum of substrates, including phosphoamide linkages.Human topoisomerase I cleavage complexes are repaired by a p53-stimulated recombination-like reaction in vitro.Neurological disorders associated with DNA strand-break processing enzymes.Poly(ADP-ribose) polymerase and XPF-ERCC1 participate in distinct pathways for the repair of topoisomerase I-induced DNA damage in mammalian cells.Effects of DNA and protein size on substrate cleavage by human tyrosyl-DNA phosphodiesterase 1.Tyrosyl-DNA Phosphodiesterase 1 (Tdp1) inhibitors Error-free and mutagenic processing of topoisomerase 1-provoked damage at genomic ribonucleotides Tyrosyl-DNA phosphodiesterase 1 (TDP1) repairs DNA damage induced by topoisomerases I and II and base alkylation in vertebrate cells.Synthesis and biological evaluation of the first dual tyrosyl-DNA phosphodiesterase I (Tdp1)-topoisomerase I (Top1) inhibitors.Repair of topoisomerase I-mediated DNA damage.Tyrosyl-DNA phosphodiesterase as a target for anticancer therapy Homologous recombination but not nucleotide excision repair plays a pivotal role in tolerance of DNA-protein cross-links in mammalian cells.Proteasome-dependent processing of topoisomerase I-DNA adducts into DNA double strand breaks at arrested replication forks.Epigenetic and genetic inactivation of tyrosyl-DNA-phosphodiesterase 1 (TDP1) in human lung cancer cells from the NCI-60 panel Structure Modeling of Human Tyrosyl-DNA Phosphodiesterase 1 and Screening for Its Inhibitors.Mechanisms of DNA-protein crosslink repair.TDP1 promotes assembly of non-homologous end joining protein complexes on DNA.Metalloprotease SPRTN/DVC1 Orchestrates Replication-Coupled DNA-Protein Crosslink Repair.Synthesis of a peptide-universal nucleotide antigen: towards next-generation antibodies to detect topoisomerase I-DNA covalent complexes.Synthesis and evaluation of the biostability and cell compatibility of novel conjugates of nucleobase, peptidic epitope, and saccharide.AP endonuclease independent repair of abasic sites in Schizosaccharomyces pombe.

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Processing of nucleopeptides mimicking the topoisomerase I-DNA covalent complex by tyrosyl-DNA phosphodiesterase

http://www.wikidata.org/entity/Q33584109

description

2002 nî lūn-bûn

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2002 թուականի Մարտին հրատարակուած գիտական յօդուած

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2002 թվականի մարտին հրատարակված գիտական հոդված

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2002年の論文

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2002年論文

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Processing of nucleopeptides m ...... tyrosyl-DNA phosphodiesterase

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Processing of nucleopeptides m ...... tyrosyl-DNA phosphodiesterase.

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Processing of nucleopeptides m ...... tyrosyl-DNA phosphodiesterase

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Processing of nucleopeptides m ...... tyrosyl-DNA phosphodiesterase

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Processing of nucleopeptides m ...... tyrosyl-DNA phosphodiesterase.

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Nucleic Acids Research

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Processing of nucleopeptides m ...... tyrosyl-DNA phosphodiesterase

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Glenda Kohlhagen

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Laurent Debéthune

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P2860

DNA T OPOISOMERASES : Structure, Function, and Mechanism

The tyrosyl-DNA phosphodiesterase Tdp1 is a member of the phospholipase D superfamily

Conservation of structure and mechanism between eukaryotic topoisomerase I and site-specific recombinases

Yeast gene for a Tyr-DNA phosphodiesterase that repairs topoisomerase I complexes.

DNA topoisomerases

Conversion of topoisomerase I cleavage complexes on the leading strand of ribosomal DNA into 5'-phosphorylated DNA double-strand breaks by replication runoff.

Topoisomerase I-mediated DNA damage.

Benzo[a]pyrene diol epoxide adducts in DNA are potent suppressors of a normal topoisomerase I cleavage site and powerful inducers of other topoisomerase I cleavages.

Induction of topoisomerase I cleavage complexes by 1-beta -D-arabinofuranosylcytosine (ara-C) in vitro and in ara-C-treated cells.

A eukaryotic enzyme that can disjoin dead-end covalent complexes between DNA and type I topoisomerases.

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1198-1204

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scholarly article

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10.1093/NAR/30.5.1198

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5

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30

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11861912

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101246

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