Gabriel Torrens
Director at esradio971.com
Periodista. De lunes a viernes, de 12 a 14h, 'Es la mañana de Baleares', en @esRadio971
Articles
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Jan 2, 2025 |
nature.com | Dibya Saha |Gabriel Torrens |Mads Hansen |Kazuki Nosho |Hannah Jeckel |Stephan Göttig | +2 more
AbstractFor any organism, survival is enhanced by the ability to sense and respond to threats in advance. For bacteria, danger sensing among kin cells has been observed, but the presence or impacts of general danger signals are poorly understood. Here we show that different bacterial species use exogenous peptidoglycan fragments, which are released by nearby kin or non-kin cell lysis, as a general danger signal.
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Nov 26, 2024 |
arxiv.org | Gabriel Torrens |Jaume Segura
arXivLabs is a framework that allows collaborators to develop and share new arXiv features directly on our website. Both individuals and organizations that work with arXivLabs have embraced and accepted our values of openness, community, excellence, and user data privacy. arXiv is committed to these values and only works with partners that adhere to them. Have an idea for a project that will add value for arXiv's community? Learn more about arXivLabs.
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Sep 29, 2024 |
es.linkedin.com | Gabriel Torrens
Gabriel Torrens’ Post Periodista y empresario, director de esRadio97.1 y presentador de 'Es la mañana de Baleares' 46m Coincidiendo con la celebración hoy del patrón de la radio, es el día de compartir las mejores noticias, apuntadas y no desveladas hasta la fecha en esta red social, ni del todo en antena.
Control of bacterial cell wall autolysins by peptidoglycan crosslinking mode - Nature Communications
Sep 11, 2024 |
nature.com | Laura Alvarez |Gabriel Torrens |Anna Weaver |Tobias Dörr
AbstractTo withstand their internal turgor pressure and external threats, most bacteria have a protective peptidoglycan (PG) cell wall. The growth of this PG polymer relies on autolysins, enzymes that create space within the structure. Despite extensive research, the regulatory mechanisms governing these PG-degrading enzymes remain poorly understood.
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Jul 3, 2024 |
nature.com | Gabriel Torrens |Rosa del Campo |André Mateus |Ana Rico |Felipe Cava |Ines Rodrigues-Lopes | +2 more
AbstractThe function of many bacterial processes depends on the formation of functional membrane microdomains (FMMs), which resemble the lipid rafts of eukaryotic cells. However, the mechanism and the biological function of these membrane microdomains remain unclear. Here, we show that FMMs in the pathogen methicillin-resistant Staphylococcus aureus (MRSA) are dedicated to confining and stabilizing proteins unfolded due to cellular stress.
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