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

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

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

http://www.wikidata.org/entity/Q24555147

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Conversion of phosphoglycolate to phosphate termini on 3' overhangs of DNA double strand breaks by the human tyrosyl-DNA phosphodiesterase hTdp1 Spinocerebellar ataxia with axonal neuropathy: consequence of a Tdp1 recessive neomorphic mutation?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 Increased expression and activity of repair genes TDP1 and XPF in non-small cell lung cancer Structure of the metal-independent restriction enzyme BfiI reveals fusion of a specific DNA-binding domain with a nonspecific nuclease Deficiency in 3'-phosphoglycolate processing in human cells with a hereditary mutation in tyrosyl-DNA phosphodiesterase (TDP1)Homologous recombination in DNA repair and DNA damage tolerance Optimal function of the DNA repair enzyme TDP1 requires its phosphorylation by ATM and/or DNA-PK The other face of restriction: modification-dependent enzymes Pathways for repairing and tolerating the spectrum of oxidative DNA lesions Drugging topoisomerases: lessons and challenges Analysis of the Active-Site Mechanism of Tyrosyl-DNA Phosphodiesterase I: A Member of the Phospholipase D Superfamily Tyrosyl-DNA phosphodiesterase (Tdp1) participates in the repair of Top2-mediated DNA damage Tyrosyl-DNA phosphodiesterase and the repair of 3'-phosphoglycolate-terminated DNA double-strand breaks.Processing of damaged DNA ends for double-strand break repair in mammalian cells 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 Recognition of phospholipids in Streptomyces phospholipase D.Design and synthesis of fluorescent substrates for human tyrosyl-DNA phosphodiesterase I.Template-directed addition of nucleosides to DNA by the BfiI restriction enzyme Identification of phosphotyrosine mimetic inhibitors of human tyrosyl-DNA phosphodiesterase I by a novel AlphaScreen high-throughput assay Inhibitors of human tyrosyl-DNA phospodiesterase (hTdp1) developed by virtual screening using ligand-based pharmacophores.Processing of nucleopeptides mimicking the topoisomerase I-DNA covalent complex by tyrosyl-DNA phosphodiesterase Spartan deficiency causes accumulation of Topoisomerase 1 cleavage complexes and tumorigenesis.Design, synthesis, and biological evaluation of O-2-modified indenoisoquinolines as dual topoisomerase I-tyrosyl-DNA phosphodiesterase I inhibitors.Yeast Tdp1 regulates the fidelity of nonhomologous end joining.Role of tyrosyl-DNA phosphodiesterase (TDP1) in mitochondria.MRE11 function in response to topoisomerase poisons is independent of its function in double-strand break repair in Saccharomyces cerevisiae The DNA binding and 3'-end preferential activity of human tyrosyl-DNA phosphodiesterase.Engineered picornavirus VPg-RNA substrates: analysis of a tyrosyl-RNA phosphodiesterase activity.SCAN1 mutant Tdp1 accumulates the enzyme--DNA intermediate and causes camptothecin hypersensitivity Tyrosyl-DNA-phosphodiesterases (TDP1 and TDP2).In vitro non-homologous DNA end joining assays--the 20th anniversary.Identification of novel PARP inhibitors using a cell-based TDP1 inhibitory assay in a quantitative high-throughput screening platform.Biochemical assays for the discovery of TDP1 inhibitors Analysis of RuvABC and RecG involvement in the escherichia coli response to the covalent topoisomerase-DNA complex DNA repair deficiency in neurodegeneration.Human Tdp1 cleaves a broad spectrum of substrates, including phosphoamide linkages.

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

http://www.wikidata.org/entity/Q24555147

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2001 nî lūn-bûn

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2001 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած

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name

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

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

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

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

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

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

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

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

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

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Proceedings of the National Academy of Sciences of the United States of America

P1476

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

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P2093

H Interthal

http://www.w3.org/2001/XMLSchema#string

J J Champoux

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J J Pouliot

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P2860

A novel family of phospholipase D homologues that includes phospholipid synthases and putative endonucleases: identification of duplicated repeats and potential active site residues

Crystal structure of a phospholipase D family member

The first crystal structure of a phospholipase D

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

A duplicated catalytic motif in a new superfamily of phosphohydrolases and phospholipid synthases that includes poxvirus envelope proteins

Biochemical and biophysical analyses of recombinant forms of human topoisomerase I

DNA topoisomerases

Mutagenesis of phospholipase D defines a superfamily including a trans-Golgi viral protein required for poxvirus pathogenicity.

Vascular factors in cognitive impairment--where are we now?

Topoisomerase I-mediated DNA damage.

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12009-14

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scholarly article

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10.1073/PNAS.211429198

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21

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98

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2001-10-09T00:00:00Z

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11775259

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11572945

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59758

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