Zobrazeno 1 - 10
of 38
pro vyhledávání: '"Alejandro Valbuena"'
Autor:
Jaime Carrasco, Rosa Antón, Alejandro Valbuena, David Pantoja-Uceda, Mayur Mukhi, Rubén Hervás, Douglas V. Laurents, María Gasset, Javier Oroz
Publikováno v:
Nature Communications, Vol 14, Iss 1, Pp 1-15 (2023)
In this work, the authors show that metamorphism in the post-translationally modified TDP-43 prion-like domain encodes determinants that command mechanisms with major relevance in disease and stress the relevance of post-translationally modified chai
Externí odkaz:
https://doaj.org/article/9a9166e33ea74700a35643c8927458e0
Autor:
Miguel Angel Fuertes, Diego López Mateos, Luis Valiente, Alicia Rodríguez Huete, Alejandro Valbuena, Mauricio G. Mateu
Publikováno v:
Viruses, Vol 15, Iss 5, p 1054 (2023)
The hollow protein capsids from a number of different viruses are being considered for multiple biomedical or nanotechnological applications. In order to improve the applied potential of a given viral capsid as a nanocarrier or nanocontainer, specifi
Externí odkaz:
https://doaj.org/article/fa52155e438e4de3b10f37f2f6cbf910
Autor:
Pablo Guerra, Alejandro Valbuena, Jordi Querol-Audí, Cristina Silva, Milagros Castellanos, Alicia Rodríguez-Huete, Damià Garriga, Mauricio G. Mateu, Nuria Verdaguer
Publikováno v:
Scientific Reports, Vol 7, Iss 1, Pp 1-13 (2017)
Abstract Recent studies reveal that the mechanical properties of virus particles may have been shaped by evolution to facilitate virus survival. Manipulation of the mechanical behavior of virus capsids is leading to a better understanding of viral in
Externí odkaz:
https://doaj.org/article/c9d7f16ea8e4443481a989e5fc02d4df
Autor:
Natalia Martín-González, Pablo Ibáñez-Freire, Álvaro Ortega-Esteban, Mara Laguna-Castro, Carmen San Martín, Alejandro Valbuena, Rafael Delgado-Buscalioni, Pedro J. de Pablo
Publikováno v:
Physical Review X, Vol 11, Iss 2, p 021025 (2021)
Icosahedral virus capsids are closed shells built up with a hexagonal lattice of proteins, which incorporate pentamers at their fivefold vertices. Human adenovirus particles lose pentamers (pentons) during infection under a variety of physicochemical
Externí odkaz:
https://doaj.org/article/0450304d917a4b97b8719ae17be46390
Autor:
Sourav Maity, Monica Mazzolini, Manuel Arcangeletti, Alejandro Valbuena, Paolo Fabris, Marco Lazzarino, Vincent Torre
Publikováno v:
Nature Communications, Vol 8, Iss 1, Pp 1-1 (2017)
Nature Communications 8: Article number: 7093 (2015); Published: 12 May 2015; Updated: 29 September 2017 An error was inadvertently introduced into the fifth sentence of the Abstract in the original version of this Article. The sentence should have s
Externí odkaz:
https://doaj.org/article/baa280c6e0204ec0a477e1af7a127c3a
Autor:
Rubén Hervás, Javier Oroz, Albert Galera-Prat, Oscar Goñi, Alejandro Valbuena, Andrés M Vera, Angel Gómez-Sicilia, Fernando Losada-Urzáiz, Vladimir N Uversky, Margarita Menéndez, Douglas V Laurents, Marta Bruix, Mariano Carrión-Vázquez
Publikováno v:
PLoS Biology, Vol 10, Iss 5, p e1001335 (2012)
Amyloidogenic neurodegenerative diseases are incurable conditions with high social impact that are typically caused by specific, largely disordered proteins. However, the underlying molecular mechanism remains elusive to established techniques. A fav
Externí odkaz:
https://doaj.org/article/ace39d0bb3a74abdb135fcb523029e9a
Autor:
Luis Valiente, Silvia López-Argüello, Alicia Rodríguez-Huete, Alejandro Valbuena, Mauricio G. Mateu
Publikováno v:
J Virol
Human rhinovirus (HRV), one of the most frequent human pathogens, is the major causative agent of common colds. HRVs also cause or exacerbate severe respiratory diseases, such as asthma or chronic obstructive pulmonary disease. Despite the biomedical
Autor:
Daniel Luque, Alvaro Ortega-Esteban, Alejandro Valbuena, Jose Luis Vilas, Alicia Rodríguez-Huete, Mauricio G. Mateu, José R. Castón
Publikováno v:
Journal of Molecular Biology. 435:168024
The biological function of macromolecular complexes depends not only on large-scale transitions between conformations, but also on small-scale conformational fluctuations at equilibrium. This study shows that detailed information on the equilibrium d
Publikováno v:
Acs Nano, 14(7), 8724-8734. AMER CHEMICAL SOC
Digital.CSIC. Repositorio Institucional del CSIC
instname
Digital.CSIC: Repositorio Institucional del CSIC
Consejo Superior de Investigaciones Científicas (CSIC)
ACS Nano
Digital.CSIC. Repositorio Institucional del CSIC
instname
Digital.CSIC: Repositorio Institucional del CSIC
Consejo Superior de Investigaciones Científicas (CSIC)
ACS Nano
Direct visualization of pathways followed by single molecules while they spontaneously self-assemble into supramolecular biological machines may provide fundamental knowledge to guide molecular therapeutics and the bottom-up design of nanomaterials a
Autor:
Santos Domínguez‐Zotes, Miguel Angel Fuertes, Alicia Rodríguez‐Huete, Alejandro Valbuena, Mauricio G Mateu
Publikováno v:
Small (Weinheim an der Bergstrasse, Germany). 18(11)
Protein-based nanostructured materials are being developed for many biomedical and nanotechnological applications. Despite their many desirable features, protein materials are highly susceptible to disruption by mechanical stress and fatigue. This st