Zobrazeno 1 - 10
of 23
pro vyhledávání: '"DNA ADP-ribosylation"'
Publikováno v:
Toxins, Vol 16, Iss 6, p 270 (2024)
Pierisin-1 was serendipitously discovered as a strong cytotoxic and apoptosis-inducing protein from pupae of the cabbage butterfly Pieris rapae against cancer cell lines. This 98-kDa protein consists of the N-terminal region (27 kDa) and C-terminal r
Externí odkaz:
https://doaj.org/article/9b4c56c50807403d88844b750556d4bb
Autor:
Andrea Hloušek-Kasun, Petra Mikolčević, Johannes Gregor Matthias Rack, Callum Tromans-Coia, Marion Schuller, Gytis Jankevicius, Marija Matković, Branimir Bertoša, Ivan Ahel, Andreja Mikoč
Publikováno v:
Computational and Structural Biotechnology Journal, Vol 20, Iss , Pp 4337-4350 (2022)
ADP-ribosylation is an ancient, highly conserved, and reversible covalent modification critical for a variety of endogenous processes in both prokaryotes and eukaryotes. ADP-ribosylation targets proteins, nucleic acids, and small molecules (including
Externí odkaz:
https://doaj.org/article/1ef90c64e4a54320bbb532d01e369a8c
Akademický článek
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Autor:
Andrea Sanchi, Giuliana Katharina Moeller, Callum Tromans-Coia, Ivan Ahel, Gyula Timinszky, Massimo Lopes
Publikováno v:
Nucleic Acids Research
ADP-ribosylation is a modification that targets a variety of macromolecules and regulates a diverse array of important cellular processes. ADP-ribosylation is catalysed by ADP-ribosyltransferases and reversed by ADP-ribosylhydrolases. Recently, an AD
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::34eb5d81443d259823f13b6d38eb72b3
https://doi.org/10.5167/uzh-217554
https://doi.org/10.5167/uzh-217554
Akademický článek
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Autor:
Takashi Oda, Toshiyuki Shimizu, Mamoru Sato, Masafumi Yamamoto, H. Minami, Kiyoshi Hiraga, Hiroshi Hashimoto, Gen Shikauchi, Keiji Wakabayashi, Ryouma Takamura, Hirokazu Hirabayashi
Publikováno v:
Journal of Biological Chemistry. 292:15445-15455
ADP-ribosyltransferases transfer the ADP-ribose moiety of βNAD+ to an acceptor molecule, usually a protein that modulates the function of the acceptor. Pierisin-1 is an ADP-ribosyltransferase from the cabbage butterfly Pieris rapae and is composed o
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3431e8dcdf0b34e6c17597fb36e2fa4f
https://doi.org/10.1074/jbc.m117.776641
https://doi.org/10.1074/jbc.m117.776641
Autor:
Hloušek-Kasun, Andrea, Mikolčević, Petra, Jankevicius, Gytis, Tromans-Coia, Callum, Sabljić, Igor, Bertoša, Branimir, Ahel, Ivan, Mikoč, Andreja
Diverse proteins that constitute ADP- ribosylation metabolic cycle have been found in bacteria from the genus Streptomyces. We focused on the macrodomain family of ADP- ribosyl hydrolases that encompass key players in the recognition, interpretation,
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=57a035e5b1ae::8854615c1c662537a9f8e5251d5d7d00
https://www.bib.irb.hr/1113383
https://www.bib.irb.hr/1113383
Autor:
Ivan Ahel, Stephan Uphoff, Emeline Lawarée, Gytis Jankevicius, Charles M. Cooper, Christoph M. Tang
Publikováno v:
Cell Reports
Cell Reports, Vol 30, Iss 5, Pp 1373-1384.e4 (2020)
Cell Reports, Vol 30, Iss 5, Pp 1373-1384.e4 (2020)
Summary ADP-ribosylation of proteins is crucial for fundamental cellular processes. Despite increasing examples of DNA ADP-ribosylation, the impact of this modification on DNA metabolism and cell physiology is unknown. Here, we show that the DarTG to
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::27e22f543acfe21c219bcd9b5c70cd42
https://doi.org/10.1016/j.celrep.2020.01.014
https://doi.org/10.1016/j.celrep.2020.01.014
Autor:
Alexander A. Ishchenko, Bakhyt T. Matkarimov, M. M. Kutuzov, Ibtissam Talhaoui, Gabriella Zarkovic, Denis Biard, Ekaterina A. Belousova, Olga I. Lavrik, Didier Gasparutto, Christine Saint-Pierre
Publikováno v:
Nucleic Acids Research
Nucleic Acids Research, Oxford University Press, 2018, 46 (5), pp.2417-2431. ⟨10.1093/nar/gkx1318⟩
Nucleic Acids Research, Oxford University Press, 2018, 46, pp.2417-2431. ⟨10.1093/nar/gkx1318⟩
Nucleic Acids Research, 2018, 46 (5), pp.2417-2431. ⟨10.1093/nar/gkx1318⟩
CONCYTEC-Institucional
Consejo Nacional de Ciencia Tecnología e Innovación Tecnológica
instacron:CONCYTEC
Nucleic Acids Research, Oxford University Press, 2018, 46 (5), pp.2417-2431. ⟨10.1093/nar/gkx1318⟩
Nucleic Acids Research, Oxford University Press, 2018, 46, pp.2417-2431. ⟨10.1093/nar/gkx1318⟩
Nucleic Acids Research, 2018, 46 (5), pp.2417-2431. ⟨10.1093/nar/gkx1318⟩
CONCYTEC-Institucional
Consejo Nacional de Ciencia Tecnología e Innovación Tecnológica
instacron:CONCYTEC
International audience; Poly(ADP-ribose) polymerases (PARPs) act as DNA break sensors and catalyze the synthesis of polymers of ADP-ribose (PAR) covalently attached to acceptor proteins at DNA damage sites. It has been demonstrated that both mammalia
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5705c405663d81735e78cf7149dc4d2e
https://hal-cea.archives-ouvertes.fr/cea-01946131
https://hal-cea.archives-ouvertes.fr/cea-01946131
Akademický článek
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