User profiles for Martín Alcorlo

martin alcorlo

Verified email at iqfr.csic.es
Cited by 932

Structural basis for the stabilization of the complement alternative pathway C3 convertase by properdin

M Alcorlo, A Tortajada… - Proceedings of the …, 2013 - National Acad Sciences
Complement is an essential component of innate immunity. Its activation results in the
assembly of unstable protease complexes, denominated C3/C5 convertases, leading to …

Class A PBPs have a distinct and unique role in the construction of the pneumococcal cell wall

…, MV Heggenhougen, M Alcorlo… - Proceedings of the …, 2020 - National Acad Sciences
In oval-shaped Streptococcus pneumoniae, septal and longitudinal peptidoglycan syntheses
are performed by independent functional complexes: the divisome and the elongasome. …

Carbohydrate recognition and lysis by bacterial peptidoglycan hydrolases

M Alcorlo, S Martínez-Caballero, R Molina… - Current opinion in …, 2017 - Elsevier
Highlights • Recent results on the structural biology of PG hydrolases reviewed. • Structural
features of PG recognition and regulation in amidases and LTs analysed. • Shared glycan …

[HTML][HTML] Structural basis of denuded glycan recognition by SPOR domains in bacterial cell division

M Alcorlo, DA Dik, S De Benedetti… - Nature …, 2019 - nature.com
SPOR domains are widely present in bacterial proteins that recognize cell-wall peptidoglycan
strands stripped of the peptide stems. This type of peptidoglycan is enriched in the septal …

Renew or die: The molecular mechanisms of peptidoglycan recycling and antibiotic resistance in Gram-negative pathogens

T Domínguez-Gil, R Molina, M Alcorlo… - Drug Resistance …, 2016 - Elsevier
Antimicrobial resistance is one of the most serious health threats. Cell-wall remodeling
processes are tightly regulated to warrant bacterial survival and in some cases are directly linked …

Structure of the large extracellular loop of FtsX and its interaction with the essential peptidoglycan hydrolase PcsB in Streptococcus pneumoniae

BE Rued, M Alcorlo, KA Edmonds… - MBio, 2019 - Am Soc Microbiol
Streptococcus pneumoniae is a leading killer of infants and immunocompromised adults and
has become increasingly resistant to major antibiotics. Therefore, the development of new …

[HTML][HTML] Modular architecture and unique teichoic acid recognition features of choline-binding protein L (CbpL) contributing to pneumococcal pathogenesis

J Gutiérrez-Fernández, M Saleh, M Alcorlo… - Scientific Reports, 2016 - nature.com
The human pathogen Streptococcus pneumoniae is decorated with a special class of
surface-proteins known as choline-binding proteins (CBPs) attached to phosphorylcholine (PCho) …

[HTML][HTML] A single amino acid polymorphism in the glycosyltransferase CpsK defines four Streptococcus suis serotypes

…, D Takamatsu, M Okura, S Teatero, M Alcorlo… - Scientific Reports, 2017 - nature.com
The capsular polysaccharide (CPS) is the major virulence factor of the emerging zoonotic
pathogen Streptococcus suis. CPS differences are also the basis for serological differentiation …

Unique structure of iC3b resolved at a resolution of 24 Å by 3D-electron microscopy

M Alcorlo, R Martínez-Barricarte… - Proceedings of the …, 2011 - National Acad Sciences
Activation of C3, deposition of C3b on the target surface, and subsequent amplification by
formation of a C3-cleaving enzyme (C3-convertase; C3bBb) triggers the effector functions of …

[HTML][HTML] Flexible structural arrangement and DNA-binding properties of protein p6 from Bacillus subtillis phage φ29

M Alcorlo, JR Luque-Ortega, F Gago… - Nucleic Acids …, 2024 - academic.oup.com
The genome-organizing protein p6 of Bacillus subtilis bacteriophage φ29 plays an essential
role in viral development by activating the initiation of DNA replication and participating in …