Listar UJI: Investigación por autoría "9e42df61-732d-4b36-a53c-06ca963b8b71"
Mostrando ítems 21-28 de 28
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Single-molecule conformational dynamics of viroporin ion channels regulated by lipid-protein interactions
Largo, Eneko; Queralt-Martín, María; Carravilla Palomanes, Pablo; Nieva, José L.; Alcaraz, Antonio Elsevier (2020-02)Classic swine fever is a highly contagious and often fatal viral disease that is caused by the classical swine fever virus (CSFV). Protein p7 of CFSV is a prototype of viroporin, a family of small, highly hydrophobic ... -
Specific adsorption of trivalent cations in biological nanopores determines conductance dynamics and reverses ionic selectivity
Queralt-Martín, María; Perini, Deborah Aurora; Alcaraz, Antonio Royal Society of Chemistry (2020-12-11)Adsorption processes are central to ionic transport in industrial and biological membrane systems. Multivalent cations modulate the conductive properties of nanofluidic devices through interactions with charged surfaces ... -
Stochastic pumping of ions based on colored noise in bacterial channels under acidic stress
López Peris, María Lidón; Queralt-Martín, María; Alcaraz, Antonio Royal Society of Chemistry (2016-06)Fluctuation-driven ion transport can be obtained in bacterial channels with the aid of different types of colored noise including the biologically relevant Lorentzian one. Using the electrochemical rectification of the ... -
Structural and functional insights into the delivery of a bacterial Rhs pore-forming toxin to the membrane
González Magaña, Amaia; Tascón, Igor; Altuna-Alvarez, Jon; Queralt-Martín, María; Colautti, Jake; Velázquez, Carmen; Zabala Zearreta, Maialen; Rojas-Palomino, Jessica; Cardenas, Marite; Alcaraz, Antonio; Whitney, John; Ubarretxena-Belandia, Iban; Albesa-Jové, David Nature Research (2023-11-28)Bacterial competition is a significant driver of toxin polymorphism, which allows continual compensatory evolution between toxins and the resistance developed to overcome their activity. Bacterial Rearrangement hot spot ... -
Surface-Functionalized Polystyrene Nanoparticles Alter the Transmembrane Potential via Ion-Selective Pores Maintaining Global Bilayer Integrity
Perini, Deborah Aurora; Parra-Ortiz, Elisa; Varó, Inmaculada; Queralt-Martín, María; Malmsten, Martin; Alcaraz, Antonio ACS Publications (2022)Although nanoplastics have well-known toxic effects toward the environment and living organisms, their molecular toxicity mechanisms, including the nature of nanoparticle−cell membrane interactions, are still under ... -
The Complex Proteolipidic Behavior of the SARS-CoV-2 Envelope Protein Channel: Weak Selectivity and Heterogeneous Oligomerization
Surya, Wahyu; Tavares Neto, Ernesto; Sanchis, Andrea; Queralt-Martín, María; Alcaraz, Antonio; Torres, Jaume; Aguilella, Vicente Multidisciplinary Digital Publishing Institute (MDPI) (2023-08-05)The envelope (E) protein is a small polypeptide that can form ion channels in coronaviruses. In SARS coronavirus 2 (SARS-CoV-2), the agent that caused the recent COVID-19 pandemic, and its predecessor SARS-CoV-1, E protein ... -
The P. aeruginosa effector Tse5 forms membrane pores disrupting the membrane potential of intoxicated bacteria
González Magaña, Amaia; Altuna, Jon; Queralt-Martín, María; Largo, Eneko; Velázquez, Carmen; Montánchez, Itxaso; Bernal, Patricia; Alcaraz, Antonio; Albesa-Jové, David Nature Research (2022)The type VI secretion system (T6SS) of Pseudomonas aeruginosa injects effector proteins into neighbouring competitors and host cells, providing a fitness advantage that allows this opportunistic nosocomial pathogen to ... -
Transport mechanisms of SARS-CoV-E viroporin in calcium solutions: Lipid-dependent Anomalous Mole Fraction Effect and regulation of pore conductance
Verdiá Báguena, Carmen; Aguilella, Vicente; Queralt-Martín, María; Alcaraz, Antonio Elsevier (2021-06-01)The envelope protein E of the SARS-CoV coronavirus is an archetype of viroporin. It is a small hydrophobic protein displaying ion channel activity that has proven highly relevant in virus-host interaction and virulence. ...