Zobrazeno 1 - 10
of 11
pro vyhledávání: '"Claudia Cericola"'
Autor:
Claudia Cericola, Alberto Luini, Alessandra Pesce, Daniela Corda, Enrico Millo, Anna Maria Massaro, Stefania Spanò, Martino Bolognesi, Marco Nardini
Publikováno v:
The EMBO Journal. 22:3122-3130
C-terminal-binding protein/brefeldin A-ADP ribosylated substrate (CtBP/BARS) plays key roles in development and oncogenesis as a transcription co-repressor, and in intracellular traffic as a promoter of Golgi membrane fission. Co-repressor activity i
Autor:
Silvio Flati, Maria G. Sciulli, Antonino Colanzi, Maria Di Girolamo, Daniela Corda, Maria Antonietta De Matteis, Julie G. Donaldson, Alexander A. Mironov, Aurora Fusella, Alberto Luini, Claudia Cericola, Giovanna Santini, Roberto Buccione, Roberto Weigert
Publikováno v:
Journal of Biological Chemistry. 272:14200-14207
Brefeldin A, a toxin inhibitor of vesicular traffic, induces the selective mono-ADP-ribosylation of two cytosolic proteins, glyceraldehyde-3-phosphate dehydrogenase and the novel GTP-binding protein BARS-50. Here, we have used a new quantitative assa
Autor:
Andrea Urbani, Claudia Cericola, Daniela Corda, Andrea R. Beccari, Maurizio Ronci, Prisca Liberali, Marco Nardini, Martino Bolognesi, Vasiliki S. Lalioti, Giuliana Catara, Carmen Valente, Agostino Bruno, Antonino Colanzi, Antonio De Flora, Alberto Luini, Giovanna Grimaldi
Publikováno v:
Proceedings of the National Academy of Sciences of the United States of America 110 (2013): 9794–9799. doi:10.1073/pnas.1222413110.
info:cnr-pdr/source/autori:Colanzi A, Grimaldi G, Catara G, Valente C, Cericola C, Liberali P, Ronci M, Lalioti VS, Bruno A, Beccari AR, Urbani A, De Flora A, Nardini M, Bolognesi M, Luini A, Corda D./titolo:Molecular mechanism and functional role of brefeldin A-mediated ADP-ribosylation of CtBP1%2FBARS./doi:10.1073%2Fpnas.1222413110./rivista:Proceedings of the National Academy of Sciences of the United States of America/anno:2013/pagina_da:9794/pagina_a:9799/intervallo_pagine:9794–9799/volume:110
Digital.CSIC. Repositorio Institucional del CSIC
instname
info:cnr-pdr/source/autori:Colanzi A, Grimaldi G, Catara G, Valente C, Cericola C, Liberali P, Ronci M, Lalioti VS, Bruno A, Beccari AR, Urbani A, De Flora A, Nardini M, Bolognesi M, Luini A, Corda D./titolo:Molecular mechanism and functional role of brefeldin A-mediated ADP-ribosylation of CtBP1%2FBARS./doi:10.1073%2Fpnas.1222413110./rivista:Proceedings of the National Academy of Sciences of the United States of America/anno:2013/pagina_da:9794/pagina_a:9799/intervallo_pagine:9794–9799/volume:110
Digital.CSIC. Repositorio Institucional del CSIC
instname
ADP-ribosylation is a posttranslational modification that modulates the functions of many target proteins. We previously showed that the fungal toxin brefeldin A (BFA) induces the ADP-ribosylation of C-terminal-binding protein-1 short-form/BFA-ADP-ri
Autor:
Antonino Colanzi, Claudia Cericola, Daniela Corda, Matteo Bonazzi, Alberto Luini, Gabriele Turacchio, Angela Persico, Cristina Hidalgo Carcedo
The Golgi ribbon is a complex structure of many stacks interconnected by tubules that undergo fragmentation during mitosis through a multistage process that allows correct Golgi inheritance. The fissioning protein CtBP1-S/BARS (BARS) is essential for
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d1e41f0e3885da60977e5edaabb33031
https://europepmc.org/articles/PMC1868899/
https://europepmc.org/articles/PMC1868899/
Autor:
Alessandra Pesce, Daniela Corda, Marco Nardini, Mauro Fasano, Francesco Secundo, Martino Bolognesi, Stefania Spanò, Dmitri I. Svergun, Chiara Bracco, Peter V. Konarev, Alberto Luini, Alessandra Donadini, Claudia Cericola
Publikováno v:
Protein science
15 (2006): 1042–1050. doi:10.1110/ps.062115406
info:cnr-pdr/source/autori:Nardini M.; Svergun D.; Konarev P.V.;, Spano S.; Fasano M.; Bracco C.; Pesce A.; Donadini A.; Cericola C.; Secundo F.; Luini A.; Corda D.; Bolognesi M./titolo:The C-terminal domain of the transcriptional corepressor CtBP is intrinsically unstructured/doi:10.1110%2Fps.062115406/rivista:Protein science (Print)/anno:2006/pagina_da:1042/pagina_a:1050/intervallo_pagine:1042–1050/volume:15
15 (2006): 1042–1050. doi:10.1110/ps.062115406
info:cnr-pdr/source/autori:Nardini M.; Svergun D.; Konarev P.V.;, Spano S.; Fasano M.; Bracco C.; Pesce A.; Donadini A.; Cericola C.; Secundo F.; Luini A.; Corda D.; Bolognesi M./titolo:The C-terminal domain of the transcriptional corepressor CtBP is intrinsically unstructured/doi:10.1110%2Fps.062115406/rivista:Protein science (Print)/anno:2006/pagina_da:1042/pagina_a:1050/intervallo_pagine:1042–1050/volume:15
C-terminal binding proteins (CtBPs) are moonlighting proteins involved in nuclear transcriptional corepression and in Golgi membrane tubule fission. Structural information on CtBPs is available for their substrate-binding domain, responsible for tran
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5050e0c9d60dc2bb598dbdb54e0f56dd
http://hdl.handle.net/11383/1499747
http://hdl.handle.net/11383/1499747
Autor:
Victor W. Hsu, Daniela Corda, Claudia Cericola, Matteo Bonazzi, Roman S. Polishchuck, Stefania Spanò, Carmen Valente, Michele Sallese, Alberto Luini, Elena V. Polishchuck, Hee Seok Kweon, Gabriele Turacchio, Antonino Colanzi, Teodoro Pulvirenti
Publikováno v:
Nature cell biology 7 (2005). doi:10.1038/ncb1260
info:cnr-pdr/source/autori:Bonazzi M.; Spanò S.; Turacchio G.; Cericola C.; Valente C.; Colanzi A.; Kweon H.S.; Hsu V.W.; Polishchuck E.V.; Polishchuck R.S.; Sallese M.; Pulvirenti T.; Corda D.; Luini A./titolo:CtBP3%2FBARS drives membrane fission in dynamin-independent transport pathways/doi:10.1038%2Fncb1260/rivista:Nature cell biology/anno:2005/pagina_da:/pagina_a:/intervallo_pagine:/volume:7
info:cnr-pdr/source/autori:Bonazzi M.; Spanò S.; Turacchio G.; Cericola C.; Valente C.; Colanzi A.; Kweon H.S.; Hsu V.W.; Polishchuck E.V.; Polishchuck R.S.; Sallese M.; Pulvirenti T.; Corda D.; Luini A./titolo:CtBP3%2FBARS drives membrane fission in dynamin-independent transport pathways/doi:10.1038%2Fncb1260/rivista:Nature cell biology/anno:2005/pagina_da:/pagina_a:/intervallo_pagine:/volume:7
Membrane fission is a fundamental step in membrane transport. So far, the only fission protein machinery that has been implicated in in vivo transport involves dynamin, and functions in several, but not all, transport pathways. Thus, other fission ma
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::550c982ea1f5b0dbd981980adbd37b98
https://publications.cnr.it/doc/184703
https://publications.cnr.it/doc/184703
Autor:
Alberto Luini, Claudia Cericola, Alessandra Pesce, Daniela Corda, Gianluca Damonte, Martino Bolognesi, Stefania Spanò, Marco Nardini
Publikováno v:
Acta crystallographica. Section D, Biological crystallography. 58(Pt 6 Pt 2)
Brefeldin A-ADP ribosylated substrate (BARS) is a newly discovered enzyme involved in membrane fission, catalyzing the formation of phosphatidic acid by transfer of an acyl group from acyl-CoA to lysophosphatidic acid. A truncated form of BARS, lacki
Autor:
Alexander A. Mironov, Cecilia Limina, Gina Sciulli, Alberto Luini, Antonino Colanzi, Maria Antonietta De Matteis, Daniela Corda, Giuseppe Di Tullio, Roberto Weigert, Claudia Cericola, Giovanna Santini
Publikováno v:
Advances in Experimental Medicine and Biology ISBN: 9781461346524
ResearcherID
ResearcherID
We have recently described a novel enzymatic mono-ADP-ribosyl transfer reaction induced by brefeldin A, a well characterized inhibitor of vesicular traffic, which selectively modifies two cytosolic proteins of 38 kDa (p38) and 50 kDa (BARS-50). p38 w
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8fbf4a4f4e597858a4ffabbd312f4911
https://doi.org/10.1007/978-1-4419-8632-0_44
https://doi.org/10.1007/978-1-4419-8632-0_44
Autor:
Matteo Bonazzi, Stefania Spanò, Gabriele Turacchio, Claudia Cericola, Carmen Valente, Antonino Colanzi, Hee Seok Kweon, Victor W. Hsu, Elena V. Polishchuck, Roman S. Polishchuck, Michele Sallese, Teodoro Pulvirenti, Daniela Corda, Alberto Luini
Publikováno v:
Nature Cell Biology. 7:637-637
Autor:
Mario Salmona, Elena V. Polishchuk, Maria Giuseppina Silletta, Daniela Corda, Gabriele Turacchio, Claudia Cericola, Stefania Spanò, Antonino Colanzi, Koert N.J. Burger, Roberto Weigert, Silvia Senatore, Francesco Facchiano, Raffaella Mancini, Alexander A. Mironov, Alberto Luini
Publikováno v:
ResearcherID
Membrane fission is essential in intracellular transport. Acyl-coenzyme As (acyl-CoAs) are important in lipid remodelling and are required for fission of COPI-coated vesicles1. Here we show that CtBP/BARS, a protein that functions in the dynamics of
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3e7d0c43160ac3d565e3cb303468e2a7
http://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcAuth=ORCID&SrcApp=OrcidOrg&DestLinkType=FullRecord&DestApp=WOS_CPL&KeyUT=WOS:000083913600061&KeyUID=WOS:000083913600061
http://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcAuth=ORCID&SrcApp=OrcidOrg&DestLinkType=FullRecord&DestApp=WOS_CPL&KeyUT=WOS:000083913600061&KeyUID=WOS:000083913600061