IBF Instituto Biofisika
Centro (uo)
University of Toronto
Toronto, CanadáPublicaciones en colaboración con investigadores/as de University of Toronto (17)
2022
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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
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Focal accumulation of aromaticity at the CDRH3 loop mitigates 4E10 polyreactivity without altering its HIV neutralization profile
iScience, Vol. 24, Núm. 9
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Guidelines for the use and interpretation of assays for monitoring autophagy (4th edition)1
Autophagy, Vol. 17, Núm. 1, pp. 1-382
2020
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Affinity for the Interface Underpins Potency of Antibodies Operating In Membrane Environments
Cell Reports, Vol. 32, Núm. 7
2019
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Molecular recognition of the native HIV-1 MPER revealed by STED microscopy of single virions
Nature Communications, Vol. 10, Núm. 1
2018
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Functional variants in the LRRK2 gene confer shared effects on risk for Crohn's disease and Parkinson's disease
Science Translational Medicine, Vol. 10, Núm. 423
2017
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Diverse Applications of Nanomedicine
ACS Nano, Vol. 11, Núm. 3, pp. 2313-2381
2016
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Specific cytoarchitectureal changes in hippocampal subareas in daDREAM mice
Molecular Brain, Vol. 9, Núm. 1
2015
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Phosphorylation-dependent changes in nucleotide binding, conformation, and dynamics of the first nucleotide binding domain (NBD1) of the sulfonylurea receptor 2B (SUR2B)
Journal of Biological Chemistry, Vol. 290, Núm. 37, pp. 22699-22714
2014
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DREAM controls the on/off switch of specific activity-dependent transcription pathways
Molecular and Cellular Biology, Vol. 34, Núm. 5, pp. 877-887
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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
2012
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NMR and fluorescence studies of drug binding to the first nucleotide binding domain of SUR2A
Biochemistry, Vol. 51, Núm. 45, pp. 9211-9222
2011
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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
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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
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Putative one-pot prebiotic polypeptides with ribonucleolytic activity
Chemistry - A European Journal, Vol. 16, Núm. 18, pp. 5314-5323
2009
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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
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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