Zobrazeno 1 - 10
of 76
pro vyhledávání: '"Gyula Timinszky"'
Autor:
Barbara Dukic, Zsófia Ruppert, Melinda E. Tóth, Ákos Hunya, Ágnes Czibula, Péter Bíró, Ádám Tiszlavicz, Mária Péter, Gábor Balogh, Miklós Erdélyi, Gyula Timinszky, László Vígh, Imre Gombos, Zsolt Török
Publikováno v:
Cells, Vol 13, Iss 13, p 1141 (2024)
Previous studies reported that a mild, non-protein-denaturing, fever-like temperature increase induced the unfolded protein response (UPR) in mammalian cells. Our dSTORM super-resolution microscopy experiments revealed that the master regulator of th
Externí odkaz:
https://doaj.org/article/c5b51908423b4e03973423dc01025547
Autor:
Joséphine Groslambert, Evgeniia Prokhorova, Anne R. Wondisford, Callum Tromans-Coia, Celeste Giansanti, Jennifer Jansen, Gyula Timinszky, Matthias Dobbelstein, Dragana Ahel, Roderick J. O’Sullivan, Ivan Ahel
Publikováno v:
Cell Reports, Vol 42, Iss 9, Pp 113113- (2023)
Summary: The timely removal of ADP-ribosylation is crucial for efficient DNA repair. However, much remains to be discovered about ADP-ribosylhydrolases. Here, we characterize the physiological role of TARG1, an ADP-ribosylhydrolase that removes aspar
Externí odkaz:
https://doaj.org/article/b876a752cfb24b1990b0c4df1c0ffbba
Autor:
Rebecca Smith, Siham Zentout, Magdalena Rother, Nicolas Bigot, Catherine Chapuis, Alexandra Mihuț, Florian Franz Zobel, Ivan Ahel, Haico van Attikum, Gyula Timinszky, Sébastien Huet
Publikováno v:
Nature Structural and Molecular Biology
Nature Structural and Molecular Biology, 2023, ⟨10.1038/s41594-023-00977-x⟩
Nature Structural and Molecular Biology, 2023, ⟨10.1038/s41594-023-00977-x⟩
International audience; Poly(ADP-ribose) polymerase 1 (PARP1) activity is regulated by its co-factor histone poly(ADP-ribosylation) factor 1 (HPF1). The complex formed by HPF1 and PARP1 catalyzes ADP-ribosylation of serine residues of proteins near D
Autor:
Edoardo José Longarini, Helen Dauben, Carolina Locatelli, Anne R. Wondisford, Rebecca Smith, Charlotte Muench, Andreas Kolvenbach, Michelle Lee Lynskey, Alexis Pope, Juan José Bonfiglio, Eva Pinto Jurado, Roberta Fajka-Boja, Thomas Colby, Marion Schuller, Ivan Ahel, Gyula Timinszky, Roderick J. O’Sullivan, Sébastien Huet, Ivan Matic
Publikováno v:
Molecular Cell
Molecular Cell, 2023, 83 (10), pp.1743-1760.e11. ⟨10.1016/j.molcel.2023.03.027⟩
Molecular Cell, 2023, 83 (10), pp.1743-1760.e11. ⟨10.1016/j.molcel.2023.03.027⟩
International audience; PARP1, an established anti-cancer target that regulates many cellular pathways, including DNA repair signaling, has been intensely studied for decades as a poly(ADP-ribosyl)transferase. Although recent studies have revealed th
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d1601d4dc993fd64a43906626e289a5e
https://hal.science/hal-04121387/file/hal-04121387.pdf
https://hal.science/hal-04121387/file/hal-04121387.pdf
Publikováno v:
AIMS Biophysics, Vol 2, Iss 4, Pp 458-475 (2015)
Chromatin has a complex, dynamic architecture in the interphase nucleus, which regulates the accessibility of the underlying DNA and plays a key regulatory role in all the cellular functions using DNA as a template, such as replication, transcription
Externí odkaz:
https://doaj.org/article/4eb6ce1830c048898c5156c5dacc9bf2
Publikováno v:
eLife, Vol 6 (2017)
The modification of serines by molecules of ADP-ribose plays an important role in signaling that the DNA in a cell has been damaged and needs to be repaired.
Externí odkaz:
https://doaj.org/article/3cd6aabf37df419b89e1ebfc08c39a79
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
PARP1 activity is regulated by its cofactor HPF1. The binding of HPF1 on PARP1 controls the grafting of ADP-ribose moieties on serine residues of proteins nearby the DNA lesions, mainly PARP1 and histones. However, the impact of HPF1 on DNA repair re
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::8dc88b4249241b42750890c7c51d8279
https://doi.org/10.1101/2021.08.27.457930
https://doi.org/10.1101/2021.08.27.457930
Autor:
Aswin Mangerich, Karla L. H. Feijs, Bernhard Lüscher, José Yélamos, Matthias Altmeyer, Bryce M. Paschal, Xiaochun Yu, Roko Zaja, Alan Ashworth, Zhao-Qi Wang, Mathias Ziegler, Nicolas C. Hoch, Susan Smith, Valina L. Dawson, George Lucian Moldovan, Guy G. Poirier, Anthony K.L. Leung, Sebastian Guettler, Christopher J. Lord, Daniela Corda, Giovanna Grimaldi, Andreas G. Ladurner, Jason Matthews, Ivan Matic, Françoise Dantzer, W. Lee Kraus, Dmitri V. Filippov, Péter Bai, Jean-Philippe Gagné, Michael O. Hottiger, John M. Pascal, Sebastian Deindl, Michael S. Cohen, Patricia Korn, Anthony R. Fehr, Mario Niepel, Joel Moss, Michael L. Nielsen, Matthew D. Daugherty, Friedrich Nolte, Krzysztof Pawłowski, Gyula Timinszky, Gioacchino Natoli, Lari Lehtiö, Ivan Ahel, Ted M. Dawson, Paul Chang
Publikováno v:
Repositório Institucional da USP (Biblioteca Digital da Produção Intelectual)
Universidade de São Paulo (USP)
instacron:USP
FEBS J
FEBS Journal
FEBS Journal, Wiley, 2021, ⟨10.1111/febs.16142⟩
The FEBS journal, vol 289, iss 23
FEBS Journal. WILEY
The FEBS Journal
Lüscher, B, Ahel, I, Altmeyer, M, Ashworth, A, Bai, P, Chang, P, Cohen, M, Corda, D, Dantzer, F, Daugherty, M D, Dawson, T M, Dawson, V L, Deindl, S, Fehr, A R, Feijs, K L H, Filippov, D V, Gagné, J P, Grimaldi, G, Guettler, S, Hoch, N C, Hottiger, M O, Korn, P, Kraus, W L, Ladurner, A, Lehtiö, L, Leung, A K L, Lord, C J, Mangerich, A, Matic, I, Matthews, J, Moldovan, G L, Moss, J, Natoli, G, Nielsen, M L, Niepel, M, Nolte, F, Pascal, J, Paschal, B M, Pawłowski, K, Poirier, G G, Smith, S, Timinszky, G, Wang, Z Q, Yélamos, J, Yu, X, Zaja, R & Ziegler, M 2022, ' ADP-ribosyltransferases, an update on function and nomenclature ', FEBS Journal, vol. 289, no. 23, pp. 7399-7410 . https://doi.org/10.1111/febs.16142
Universidade de São Paulo (USP)
instacron:USP
FEBS J
FEBS Journal
FEBS Journal, Wiley, 2021, ⟨10.1111/febs.16142⟩
The FEBS journal, vol 289, iss 23
FEBS Journal. WILEY
The FEBS Journal
Lüscher, B, Ahel, I, Altmeyer, M, Ashworth, A, Bai, P, Chang, P, Cohen, M, Corda, D, Dantzer, F, Daugherty, M D, Dawson, T M, Dawson, V L, Deindl, S, Fehr, A R, Feijs, K L H, Filippov, D V, Gagné, J P, Grimaldi, G, Guettler, S, Hoch, N C, Hottiger, M O, Korn, P, Kraus, W L, Ladurner, A, Lehtiö, L, Leung, A K L, Lord, C J, Mangerich, A, Matic, I, Matthews, J, Moldovan, G L, Moss, J, Natoli, G, Nielsen, M L, Niepel, M, Nolte, F, Pascal, J, Paschal, B M, Pawłowski, K, Poirier, G G, Smith, S, Timinszky, G, Wang, Z Q, Yélamos, J, Yu, X, Zaja, R & Ziegler, M 2022, ' ADP-ribosyltransferases, an update on function and nomenclature ', FEBS Journal, vol. 289, no. 23, pp. 7399-7410 . https://doi.org/10.1111/febs.16142
ADP-ribosylation, a modification of proteins, nucleic acids and metabolites, confers broad functions, including roles in stress responses elicited for example by DNA damage and viral infection and is involved in intra- and extracellular signaling, ch
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::630b65b016239f43979422dfa49f94cd
Publikováno v:
PLoS ONE, Vol 3, Iss 6, p e2506 (2008)
BACKGROUND: Germline progenitors resist signals that promote differentiation into somatic cells. This occurs through the transient repression in primordial germ cells of RNA polymerase II, specifically by disrupting Ser2 phosphorylation on its C-term
Externí odkaz:
https://doaj.org/article/af285f8bd2b9429f92c9155aa91be495