Structural basis for DNA 3′-end processing by human tyrosyl-DNA phosphodiesterase 1

Human tyrosyl-DNA phosphodiesterase 1 (Tdp1) repairs covalently trapped topoisomerase 1B-DNA complexes and other lesions, and is a target for anticancer drug development. Here the authors use an integrated structural approach to shed light onto the molecular basis of DNA end-processing by Tdp1.

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Autores principales:	Fiona J. Flett, Emilija Ruksenaite, Lee A. Armstrong, Shipra Bharati, Roberta Carloni, Elizabeth R. Morris, C. Logan Mackay, Heidrun Interthal, Julia M. Richardson
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2018
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/2dff6c27b8244f03bdfbb18f51738a7b
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spelling	oai:doaj.org-article:2dff6c27b8244f03bdfbb18f51738a7b2021-12-02T17:33:17ZStructural basis for DNA 3′-end processing by human tyrosyl-DNA phosphodiesterase 110.1038/s41467-017-02530-z2041-1723https://doaj.org/article/2dff6c27b8244f03bdfbb18f51738a7b2018-01-01T00:00:00Zhttps://doi.org/10.1038/s41467-017-02530-zhttps://doaj.org/toc/2041-1723Human tyrosyl-DNA phosphodiesterase 1 (Tdp1) repairs covalently trapped topoisomerase 1B-DNA complexes and other lesions, and is a target for anticancer drug development. Here the authors use an integrated structural approach to shed light onto the molecular basis of DNA end-processing by Tdp1.Fiona J. FlettEmilija RuksenaiteLee A. ArmstrongShipra BharatiRoberta CarloniElizabeth R. MorrisC. Logan MackayHeidrun InterthalJulia M. RichardsonNature PortfolioarticleScienceQENNature Communications, Vol 9, Iss 1, Pp 1-13 (2018)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Fiona J. Flett Emilija Ruksenaite Lee A. Armstrong Shipra Bharati Roberta Carloni Elizabeth R. Morris C. Logan Mackay Heidrun Interthal Julia M. Richardson Structural basis for DNA 3′-end processing by human tyrosyl-DNA phosphodiesterase 1
description	Human tyrosyl-DNA phosphodiesterase 1 (Tdp1) repairs covalently trapped topoisomerase 1B-DNA complexes and other lesions, and is a target for anticancer drug development. Here the authors use an integrated structural approach to shed light onto the molecular basis of DNA end-processing by Tdp1.
format	article
author	Fiona J. Flett Emilija Ruksenaite Lee A. Armstrong Shipra Bharati Roberta Carloni Elizabeth R. Morris C. Logan Mackay Heidrun Interthal Julia M. Richardson
author_facet	Fiona J. Flett Emilija Ruksenaite Lee A. Armstrong Shipra Bharati Roberta Carloni Elizabeth R. Morris C. Logan Mackay Heidrun Interthal Julia M. Richardson
author_sort	Fiona J. Flett
title	Structural basis for DNA 3′-end processing by human tyrosyl-DNA phosphodiesterase 1
title_short	Structural basis for DNA 3′-end processing by human tyrosyl-DNA phosphodiesterase 1
title_full	Structural basis for DNA 3′-end processing by human tyrosyl-DNA phosphodiesterase 1
title_fullStr	Structural basis for DNA 3′-end processing by human tyrosyl-DNA phosphodiesterase 1
title_full_unstemmed	Structural basis for DNA 3′-end processing by human tyrosyl-DNA phosphodiesterase 1
title_sort	structural basis for dna 3′-end processing by human tyrosyl-dna phosphodiesterase 1
publisher	Nature Portfolio
publishDate	2018
url	https://doaj.org/article/2dff6c27b8244f03bdfbb18f51738a7b
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Structural basis for DNA 3′-end processing by human tyrosyl-DNA phosphodiesterase 1

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