Zobrazeno 1 - 10
of 32
pro vyhledávání: '"Heidrun Interthal"'
Autor:
Fiona J. Flett, Emilija Ruksenaite, Lee A. Armstrong, Shipra Bharati, Roberta Carloni, Elizabeth R. Morris, C. Logan Mackay, Heidrun Interthal, Julia M. Richardson
Publikováno v:
Nature Communications, Vol 9, Iss 1, Pp 1-13 (2018)
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 m
Externí odkaz:
https://doaj.org/article/2dff6c27b8244f03bdfbb18f51738a7b
Publikováno v:
Edwards, E R, Interthal, H & McQueen, H A 2021, ' Managing your mind : How simple activities within the curriculum can improve undergraduate students’ mental health and well-being ', New Directions in the Teaching of Physical Sciences, vol. 16, no. 1 . https://doi.org/10.29311/ndtps.v0i16.3588
The transition into higher education stretches students socially, academically and within their personal lives requiring adaptation and development of resilience. For many, such demands may lead to decreased mental well-being and, for some, mental il
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::cbd99a9f2be5032d031fcceece0c12bd
https://www.pure.ed.ac.uk/ws/files/202588519/3588_10774_1_PB.pdf
https://www.pure.ed.ac.uk/ws/files/202588519/3588_10774_1_PB.pdf
Autor:
Jianghong An, Yoko Shimizu, Tom A. Pfeifer, Hok Khim Fam, Cornelius F. Boerkoel, Kunho Choi, Richard A. Dean, Heidrun Interthal, Steven J.M. Jones
Publikováno v:
SLAS Discovery. 19:1372-1382
Mutations of DNA repair pathways contribute to tumorigenesis and provide a therapeutic target for synthetic lethal interactions in tumor cells. Given that tyrosyl-DNA phosphodiesterase 1 (Tdp1) repairs stalled topoisomerase-I DNA complexes, we hypoth
Publikováno v:
Analytical chemistry. 89(21)
Cross-linking of nucleic acids to proteins in combination with mass spectrometry permits the precise identification of interacting residues between nucleic acid-protein complexes. However, the mass spectrometric identification and characterization of
Autor:
Fiona J, Flett, Emilija, Ruksenaite, Lee A, Armstrong, Shipra, Bharati, Roberta, Carloni, Elizabeth R, Morris, C Logan, Mackay, Heidrun, Interthal, Julia M, Richardson
Publikováno v:
Nature Communications
Tyrosyl-DNA phosphodiesterase (Tdp1) is a DNA 3′-end processing enzyme that repairs topoisomerase 1B-induced DNA damage. We use a new tool combining site-specific DNA–protein cross-linking with mass spectrometry to identify Tdp1 interactions with
Publikováno v:
Analytical chemistry. 87(19)
UV cross-linking of nucleic acids to proteins in combination with mass spectrometry is a powerful technique to identify proteins, peptides, and the amino acids involved in intermolecular interactions within nucleic acid-protein complexes. However, th
Publikováno v:
Journal of Medicinal Chemistry. 47:829-837
Tyrosyl-DNA phosphodiesterase (Tdp1) catalyzes the hydrolysis of a phosphodiester bond between a tyrosine residue and a DNA 3' phosphate and functions as a DNA repair enzyme that cleaves stalled topoisomerase I-DNA complexes. We previously determined
Publikováno v:
Journal of Biological Chemistry. 279:2984-2992
Based on co-crystal structures of human topoisomerase I with bound DNA, Lys(532) makes a minor groove contact with the strongly preferred thymidine residue at the site of covalent attachment (-1 position). Replacement of Lys(532) with either arginine
Publikováno v:
Journal of Molecular Biology. 324:917-932
Tyrosyl-DNA phosphodiesterase (Tdp1) is a DNA repair enzyme that catalyzes the hydrolysis of a phosphodiester bond between a tyrosine residue and a DNA 3′-phosphate. The only known example of such a linkage in eukaryotic cells occurs normally as a
Publikováno v:
Structure. 10:237-248
Tyrosyl-DNA phosphodiesterase (Tdp1) catalyzes the hydrolysis of a phosphodiester bond between a tyrosine residue and a DNA 3′ phosphate. The enzyme appears to be responsible for repairing the unique protein-DNA linkage that occurs when eukaryotic