Zobrazeno 1 - 10
of 58
pro vyhledávání: '"Giovanna Grimaldi"'
Autor:
Annunziata Corteggio, Matteo Lo Monte, Laura Schembri, Nina Dathan, Simone Di Paola, Giovanna Grimaldi, Daniela Corda
The GTPase Rab14 is localized at the trans-Golgi network and at the intermediate compartment associated to sorting/recycling endosomes-like structures of the transferrin-recycling pathway: as other Rab family members, it is involved in the regulation
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::f7462a075a8296c7d9f0ee4370823969
https://doi.org/10.1101/2022.11.26.517555
https://doi.org/10.1101/2022.11.26.517555
Autor:
Simone Di Paola, Maria Matarese, Maria Luisa Barretta, Nina Dathan, Antonino Colanzi, Daniela Corda, Giovanna Grimaldi
Publikováno v:
Cancers; Volume 14; Issue 21; Pages: 5210
Intracellular mono-ADP-ribosyltransferases (mono-ARTs) catalyze the covalent attachment of a single ADP-ribose molecule to protein substrates, thus regulating their functions. PARP10 is a soluble mono-ART involved in the modulation of intracellular s
Autor:
Giovanna Grimaldi, Angela Filograna, Laura Schembri, Matteo Lo Monte, Rosaria Di Martino, Marinella Pirozzi, Daniela Spano, Andrea R. Beccari, Seetharaman Parashuraman, Alberto Luini, Carmen Valente, Daniela Corda
Publikováno v:
Proceedings of the National Academy of Sciences of the United States of America
Significance Proteins are modified by many posttranslational modifications (PTMs) with crucial regulatory functions. A PTM attracting increasing interest is ADP-ribosylation, capable of altering crucial cellular targets. We show that mono-ADP-ribosyl
Autor:
Daniela Corda, Giovanna Grimaldi, Luca Palazzo, Carmen Valente, Annunziata Corteggio, Giuliana Catara
Publikováno v:
Biochemical pharmacology 167 (2019): 64–75. doi:10.1016/j.bcp.2019.05.019
info:cnr-pdr/source/autori:Grimaldi, Giovanna; Catara, Giuliana; Palazzo, Luca; Corteggio, Annunziata; Valente, Carmen; Corda, Daniela/titolo:PARPs and PAR as novel pharmacological targets for the treatment of stress granule-associated disorders/doi:10.1016%2Fj.bcp.2019.05.019/rivista:Biochemical pharmacology/anno:2019/pagina_da:64/pagina_a:75/intervallo_pagine:64–75/volume:167
info:cnr-pdr/source/autori:Grimaldi, Giovanna; Catara, Giuliana; Palazzo, Luca; Corteggio, Annunziata; Valente, Carmen; Corda, Daniela/titolo:PARPs and PAR as novel pharmacological targets for the treatment of stress granule-associated disorders/doi:10.1016%2Fj.bcp.2019.05.019/rivista:Biochemical pharmacology/anno:2019/pagina_da:64/pagina_a:75/intervallo_pagine:64–75/volume:167
Among the post-translational modifications, ADP-ribosylation has been for long time the least integrated in the scheme of the structural protein modifications affecting physiological functions. In spite of the original findings on bacterial-dependent
Autor:
Daniela Corda, Giovanna Grimaldi
Publikováno v:
Biochemical Society transactions 47 (2019): 357–370. doi:10.1042/BST20180416
info:cnr-pdr/source/autori:Grimaldi, Giovanna; Corda, Daniela/titolo:ADP-ribosylation and intracellular traffic: an emerging role for PARP enzymes/doi:10.1042%2FBST20180416/rivista:Biochemical Society transactions/anno:2019/pagina_da:357/pagina_a:370/intervallo_pagine:357–370/volume:47
info:cnr-pdr/source/autori:Grimaldi, Giovanna; Corda, Daniela/titolo:ADP-ribosylation and intracellular traffic: an emerging role for PARP enzymes/doi:10.1042%2FBST20180416/rivista:Biochemical Society transactions/anno:2019/pagina_da:357/pagina_a:370/intervallo_pagine:357–370/volume:47
ADP-ribosylation is an ancient and reversible post-translational modification (PTM) of proteins, in which the ADP-ribose moiety is transferred from NAD+ to target proteins by members of poly-ADP-ribosyl polymerase (PARP) family. The 17 members of thi
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
Autor:
Andrea R. Beccari, Daniela Corda, Giovanna Grimaldi, Daniela Spano, Matteo Lo Monte, Schembri L, Carmen Valente, Di Martino R
Publikováno v:
bioRxiv the preprint server for biology (2020). doi:10.1101/2020.05.05.078097
info:cnr-pdr/source/autori:Giovanna Grimaldi, Laura Schembri, Matteo Lo Monte, Daniela Spano, Rosaria Di Martino, Andrea R Beccari, Carmen Valente, Daniela Corda/titolo:PARP12-catalyzed mono-ADP-ribosylation of Golgin-97 controls the transport of E-cadherin/doi:10.1101%2F2020.05.05.078097/rivista:bioRxiv the preprint server for biology/anno:2020/pagina_da:/pagina_a:/intervallo_pagine:/volume
info:cnr-pdr/source/autori:Giovanna Grimaldi, Laura Schembri, Matteo Lo Monte, Daniela Spano, Rosaria Di Martino, Andrea R Beccari, Carmen Valente, Daniela Corda/titolo:PARP12-catalyzed mono-ADP-ribosylation of Golgin-97 controls the transport of E-cadherin/doi:10.1101%2F2020.05.05.078097/rivista:bioRxiv the preprint server for biology/anno:2020/pagina_da:/pagina_a:/intervallo_pagine:/volume
ADP-ribosylation is a post-translational modification involved in physiological and pathological events catalyzed by Poly-ADP-Ribosyl-Polymerase (PARP) enzymes. Substrates of this reaction have been identified by mass-spectrometry, but the definition
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4acbcffc7df215d9fd85e330568bcc01
Autor:
Daniela Corda, Laura Schembri, Carmen Valente, Giuliana Catara, Daniela Spano, Matteo Lo Monte, Gabriele Turacchio, Andrea R. Beccari, Giovanna Grimaldi
Publikováno v:
Scientific Reports, Vol 7, Iss 1, Pp 1-17 (2017)
Scientific reports (Nature Publishing Group) 7 (2017). doi:10.1038/s41598-017-14156-8
info:cnr-pdr/source/autori:Catara, Giuliana; Grimaldi, Giovanna; Schembri, Laura; Spano, Daniela; Turacchio, Gabriele; Lo Monte, Matteo; Beccari, Andrea Rosario; Valente, Carmen; Corda, Daniela/titolo:PARP1-produced poly-ADP-ribose causes the PARP12 translocation to stress granules and impairment of Golgi complex functions/doi:10.1038%2Fs41598-017-14156-8/rivista:Scientific reports (Nature Publishing Group)/anno:2017/pagina_da:/pagina_a:/intervallo_pagine:/volume:7
Scientific Reports
Scientific reports (Nature Publishing Group) 7 (2017). doi:10.1038/s41598-017-14156-8
info:cnr-pdr/source/autori:Catara, Giuliana; Grimaldi, Giovanna; Schembri, Laura; Spano, Daniela; Turacchio, Gabriele; Lo Monte, Matteo; Beccari, Andrea Rosario; Valente, Carmen; Corda, Daniela/titolo:PARP1-produced poly-ADP-ribose causes the PARP12 translocation to stress granules and impairment of Golgi complex functions/doi:10.1038%2Fs41598-017-14156-8/rivista:Scientific reports (Nature Publishing Group)/anno:2017/pagina_da:/pagina_a:/intervallo_pagine:/volume:7
Scientific Reports
Poly-ADP-ribose-polymerases (PARPs) 1 and 2 are nuclear enzymes that catalyze the poly-ADP-ribosylation of nuclear proteins transferring poly-ADP-ribose (PAR) polymers to specific residues. PARPs and PAR intervene in diverse functions, including DNA
Publikováno v:
Biochemical Pharmacology
Biochemical pharmacology 167 (2019): 13–26. doi:10.1016/j.bcp.2019.06.001
info:cnr-pdr/source/autori:Catara, Giuliana; Corteggio, Annunziata; Valente, Carmen; Grimaldi, Giovanna; Palazzo, Luca/titolo:Targeting ADP-ribosylation as an antimicrobial strategy/doi:10.1016%2Fj.bcp.2019.06.001/rivista:Biochemical pharmacology/anno:2019/pagina_da:13/pagina_a:26/intervallo_pagine:13–26/volume:167
Biochemical pharmacology 167 (2019): 13–26. doi:10.1016/j.bcp.2019.06.001
info:cnr-pdr/source/autori:Catara, Giuliana; Corteggio, Annunziata; Valente, Carmen; Grimaldi, Giovanna; Palazzo, Luca/titolo:Targeting ADP-ribosylation as an antimicrobial strategy/doi:10.1016%2Fj.bcp.2019.06.001/rivista:Biochemical pharmacology/anno:2019/pagina_da:13/pagina_a:26/intervallo_pagine:13–26/volume:167
Graphical abstract
ADP-ribosylation (ADPr) is an ancient reversible modification of cellular macromolecules controlling major biological processes as diverse as DNA damage repair, transcriptional regulation, intracellular transport, immune and s
ADP-ribosylation (ADPr) is an ancient reversible modification of cellular macromolecules controlling major biological processes as diverse as DNA damage repair, transcriptional regulation, intracellular transport, immune and s
Publikováno v:
Methods in molecular biology (Clifton, N.J.). 1813
ADP-ribosylation is a post-translational modification of proteins that has required the development of specific technical approaches for the full definition of its physiological roles and regulation. The identification of the enzymes and specific sub