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Trends in Pharmacological Sciences|July 3, 2021
Teaching an old dog new tricks: repurposing β-lactamsVega Miguel-Ruano, Juan A Hermoso
ACS Omega|October 27, 2025
Structural Characterization of Lytic Transglycosylase SltB2 of <i>Pseudomonas aeruginosa</i>Vega Miguel-Ruano, María T Batuecas, Elena Lastochkin, et al.
Nature Communications|February 13, 2024
A distinctive family of L,D-transpeptidases catalyzing L-Ala-mDAP crosslinks in Alpha- and BetaproteobacteriaAkbar Espaillat, Laura Alvarez, Gabriel Torrens, et al.
International Journal of Biological Macromolecules|April 7, 2024
Structural characterization of lytic transglycosylase MltD of Pseudomonas aeruginosa, a target for the natural product bulgecin AVega Miguel-Ruano, Rhona Feltzer, María T Batuecas, et al.
Infection and Immunity|July 31, 2025
Structural and functional characterization of IdeC, a novel IgG-specific protease of <i>Streptococcus canis</i>Saoirse Walsh, Antje-Maria Lapschies, Vega Miguel-Ruano, et al.
Journal of the American Chemical Society|May 8, 2026
Outer Membrane-Peptidoglycan Anchoring in <i>Pseudomonas aeruginosa</i>Amr M El-Araby, Uxía Pérez de José, Vega Miguel-Ruano, et al.
Nature Communications|July 11, 2023
DipM controls multiple autolysins and mediates a regulatory feedback loop promoting cell constriction in Caulobacter crescentusAdrian Izquierdo-Martinez, Maria Billini, Vega Miguel-Ruano, et al.
Computational and Structural Biotechnology Journal|March 8, 2021
Biochemical and Structural Characterization of a novel thermophilic esterase EstD11 provide catalytic insights for the HSL familyVega Miguel-Ruano, Ivanna Rivera, Jelena Rajkovic, et al.
ACS Catalysis|December 26, 2024
Characterization of VldE (Spr1875), a Pneumococcal Two-State l,d-Endopeptidase with a Four-Zinc Cluster in the Active SiteVega Miguel-Ruano, Iván Acebrón, Mijoon Lee, et al.
Nature Chemical Biology|July 26, 2024
Restoring susceptibility to β-lactam antibiotics in methicillin-resistant Staphylococcus aureusVan T Nguyen, Biruk T Birhanu, Vega Miguel-Ruano, et al.
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