Publicaciones en colaboración con investigadoras/es de University of Toronto (14)

2024

  1. The Human Phenotype Ontology in 2024: phenotypes around the world

    Nucleic acids research, Vol. 52, Núm. D1, pp. D1333-D1346

2022

  1. Engineering pan-HIV-1 neutralization potency through multispecific antibody avidity

    Proceedings of the National Academy of Sciences of the United States of America, Vol. 119, Núm. 4

2021

  1. Focal accumulation of aromaticity at the CDRH3 loop mitigates 4E10 polyreactivity without altering its HIV neutralization profile

    iScience, Vol. 24, Núm. 9

  2. Guidelines for the use and interpretation of assays for monitoring autophagy (4th edition)1

    Autophagy, Vol. 17, Núm. 1, pp. 1-382

2020

  1. Affinity for the Interface Underpins Potency of Antibodies Operating In Membrane Environments

    Cell Reports, Vol. 32, Núm. 7

2019

  1. Molecular recognition of the native HIV-1 MPER revealed by STED microscopy of single virions

    Nature Communications, Vol. 10, Núm. 1

2017

  1. Diverse Applications of Nanomedicine

    ACS Nano, Vol. 11, Núm. 3, pp. 2313-2381

2014

  1. A unified nomenclature and amino acid numbering for human PTEN

    Science Signaling, Vol. 7, Núm. 332

  2. Structure and immunogenicity of a peptide vaccine, including the complete HIV-1 gp41 2F5 epitope: Implications for antibody recognition mechanism and immunogen design

    Journal of Biological Chemistry, Vol. 289, Núm. 10, pp. 6565-6580

2011

  1. Exclusion of the GNAS locus in PHP-Ib patients with broad GNAS methylation changes: Evidence for an autosomal recessive form of PHP-Ib?

    Journal of Bone and Mineral Research, Vol. 26, Núm. 8, pp. 1854-1863

  2. Interaction of anti-HIV type 1 antibody 2F5 with phospholipid bilayers and its relevance for the mechanism of virus neutralization

    AIDS Research and Human Retroviruses, Vol. 27, Núm. 8, pp. 863-876

2010

  1. Ablation of the complementarity-determining region H3 apex of the anti-HIV-1 broadly neutralizing antibody 2F5 abrogates neutralizing capacity without affecting core epitope binding

    Journal of Virology, Vol. 84, Núm. 9, pp. 4136-4147

2009

  1. Structural Constraints Imposed by the Conserved Fusion Peptide on the HIV-1 gp41 Epitope Recognized by the Broadly Neutralizing Antibody 2F5

    Journal of Physical Chemistry B, Vol. 113, Núm. 41, pp. 13626-13637

2008

  1. Structural Details of HIV-1 Recognition by the Broadly Neutralizing Monoclonal Antibody 2F5: Epitope Conformation, Antigen-Recognition Loop Mobility, and Anion-Binding Site

    Journal of Molecular Biology, Vol. 384, Núm. 2, pp. 377-392