Zobrazeno 1 - 10
of 88
pro vyhledávání: '"Gonzalo de Prat-Gay"'
Autor:
Araceli Visentin, Nicolás Demitroff, Mariano Salgueiro, Silvia Susana Borkosky, Vladimir N. Uversky, Gabriela Camporeale, Gonzalo de Prat-Gay
Publikováno v:
Viruses, Vol 15, Iss 6, p 1329 (2023)
A wide variety of viruses replicate in liquid-like viral factories. Non-segmented negative stranded RNA viruses share a nucleoprotein (N) and a phosphoprotein (P) that together emerge as the main drivers of liquid–liquid phase separation. The respi
Externí odkaz:
https://doaj.org/article/132b45b52c35464c9d069556a9355325
Autor:
Nora Lopez, Gabriela Camporeale, Mariano Salgueiro, Silvia Susana Borkosky, Araceli Visentín, Ramon Peralta-Martinez, María Eugenia Loureiro, Gonzalo de Prat-Gay
Publikováno v:
PLoS Pathogens, Vol 17, Iss 10, p e1009926 (2021)
Viruses have evolved precise mechanisms for using the cellular physiological pathways for their perpetuation. These virus-driven biochemical events must be separated in space and time from those of the host cell. In recent years, granular structures,
Externí odkaz:
https://doaj.org/article/7530452a7b9643dd93f5a3bd477c7a2a
Publikováno v:
PLoS ONE, Vol 8, Iss 9, p e74338 (2013)
Human respiratory syncytial virus (hRSV) is a major infectious agent that cause pediatric respiratory disease worldwide. Considered one of the main virulence factors of hRSV, NS1 is known to suppress type I interferon response and signaling, thus fav
Externí odkaz:
https://doaj.org/article/753b6f0e8df2407cb8efc799051cc00e
Autor:
María G Noval, Mariana Gallo, Sebastián Perrone, Andres G Salvay, Lucía B Chemes, Gonzalo de Prat-Gay
Publikováno v:
PLoS ONE, Vol 8, Iss 9, p e72760 (2013)
Intrinsic disorder is abundant in viral genomes and provides conformational plasticity to its protein products. In order to gain insight into its structure-function relationships, we carried out a comprehensive analysis of structural propensities wit
Externí odkaz:
https://doaj.org/article/70aae980d29d464bbe21dc27106f0177
Autor:
Lucía B Chemes, Juliana Glavina, Leonardo G Alonso, Cristina Marino-Buslje, Gonzalo de Prat-Gay, Ignacio E Sánchez
Publikováno v:
PLoS ONE, Vol 7, Iss 10, p e47661 (2012)
In the present work, we have used the papillomavirus E7 oncoprotein to pursue structure-function and evolutionary studies that take into account intrinsic disorder and the conformational diversity of globular domains. The intrinsically disordered (E7
Externí odkaz:
https://doaj.org/article/5e084f0c6dd747988b5c7fdb4fc1858d
Autor:
Mariano Salgueiro, Gabriela Camporeale, Araceli Visentin, Martin Aran, Leonardo Pellizza, Sebastián Esperante, Agustín Corbat, Hernán Grecco, Belén Sousa, Ramiro Esperón, Silvia S. Borkosky, Gonzalo de Prat-Gay
Publikováno v:
Journal of Molecular Biology. :168153
Viral factories of liquid-like nature host transcription and replication in most viruses. The syncytial respiratory virus factories include gene function proteins, brought together by the phosphoprotein (P) RNA polymerase cofactor, present across non
Autor:
Silvia Susana Borkosky, Marisol Fassolari, Karen Campos-León, Andrés Hugo Rossi, Mariano Salgueiro, Carla Pascuale, Ramón Peralta Martínez, Kevin Gaston, Gonzalo de Prat Gay
As guardian of the genome, p53 exerts its tumor suppressor activity by modulating the expression of several hundreds of genes and by interacting with a large number of proteins. However, p53 can also repress viral replication and it is targeted by a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::ba34a3d2c4747262077f1697eee9a666
https://doi.org/10.1101/2022.02.09.479752
https://doi.org/10.1101/2022.02.09.479752
Autor:
Nicolás S. González-Foutel, Juliana Glavina, Wade M. Borcherds, Matías Safranchik, Susana Barrera-Vilarmau, Amin Sagar, Alejandro Estaña, Amelie Barozet, Nicolás A. Garrone, Gregorio Fernandez-Ballester, Clara Blanes-Mira, Ignacio E. Sánchez, Gonzalo de Prat-Gay, Juan Cortés, Pau Bernadó, Rohit V. Pappu, Alex S. Holehouse, Gary W. Daughdrill, Lucía B. Chemes
Publikováno v:
Digital.CSIC. Repositorio Institucional del CSIC
instname
Nat Struct Mol Biol
Nature Structural and Molecular Biology
Nature Structural and Molecular Biology, 2022, 29 (8), pp.781-790. ⟨10.1038/s41594-022-00811-w⟩
instname
Nat Struct Mol Biol
Nature Structural and Molecular Biology
Nature Structural and Molecular Biology, 2022, 29 (8), pp.781-790. ⟨10.1038/s41594-022-00811-w⟩
Many disordered proteins conserve essential functions in the face of extensive sequence variation, making it challenging to identify the mechanisms responsible for functional selection. Here we identify the molecular mechanism of functional selection
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7f5686ad3777728c8721b6deba4c2af8
https://api.elsevier.com/content/abstract/scopus_id/85135867846
https://api.elsevier.com/content/abstract/scopus_id/85135867846
Autor:
Silvia S. Borkosky, Gabriela Camporeale, Araceli Visentin, María Eugenia Loureiro, Nora Lopez, Gonzalo de Prat-Gay, Mariano Salgueiro, Ramon Peralta-Martinez
Publikováno v:
PLoS Pathogens
PLoS Pathogens, Vol 17, Iss 10, p e1009926 (2021)
PLoS Pathogens, Vol 17, Iss 10, p e1009926 (2021)
Viruses have evolved precise mechanisms for using the cellular physiological pathways for their perpetuation. These virus-driven biochemical events must be separated in space and time from those of the host cell. In recent years, granular structures,
Autor:
Gary W. Daughdrill, Wade Borcherds, Alex S. Holehouse, Ignacio E. Sánchez, Clara Blanes-Mira, Alejandro Estaña, Susana Barrera-Vilarmau, Amin Sagar, Gregorio Fernández-Ballester, Juan Cortés, Pau Bernadó, Rohit V. Pappu, Amélie Barozet, Juliana Glavina, Gonzalo de Prat-Gay, Lucía B. Chemes, Nicolas S. Gonzalez-Foutel
Many disordered proteins conserve essential functions in the face of extensive sequence variation. This makes it challenging to identify the forces responsible for functional selection. Viruses are robust model systems to investigate functional selec
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::74353c0c8cc7af904aedc731bc0f6b34
https://doi.org/10.1101/2021.05.14.444182
https://doi.org/10.1101/2021.05.14.444182