Publicaciones en las que colabora con JOSE LUIS NIEVA ESCANDON (24)

2024

  1. A two-step mechanism for the binding of the HIV-1 MPER epitope by the 10E8 antibody onto biosensor-supported lipid bilayers

    FEBS Letters, Vol. 598, Núm. 7, pp. 787-800

  2. Liposome-based peptide vaccines to elicit immune responses against the membrane active domains of the HIV-1 Env glycoprotein

    Biochimica et Biophysica Acta - Biomembranes, Vol. 1866, Núm. 1

2022

  1. Functional Delineation of a Protein-Membrane Interaction Hotspot Site on the HIV-1 Neutralizing Antibody 10E8

    International journal of molecular sciences, Vol. 23, Núm. 18

  2. Molecular recognition of a membrane-anchored HIV-1 pan-neutralizing epitope

    Communications Biology, Vol. 5, Núm. 1

2021

  1. Conformational plasticity underlies membrane fusion induced by an HIV sequence juxtaposed to the lipid envelope

    Scientific Reports, Vol. 11, Núm. 1

2020

  1. Cholesterol Constrains the Antigenic Configuration of the Membrane-Proximal Neutralizing HIV-1 Epitope

    ACS infectious diseases, Vol. 6, Núm. 8, pp. 2155-2168

2019

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

    Nature Communications, Vol. 10, Núm. 1

2018

  1. Exposure of the HIV-1 broadly neutralizing antibody 10E8 MPER epitope on the membrane surface by gp41 transmembrane domain scaffolds

    Biochimica et Biophysica Acta - Biomembranes, Vol. 1860, Núm. 6, pp. 1259-1271

2017

  1. Effects of HIV-1 gp41-Derived Virucidal Peptides on Virus-like Lipid Membranes

    Biophysical Journal, Vol. 113, Núm. 6, pp. 1301-1310

2016

  1. Structural basis for broad neutralization of HIV-1 through the molecular recognition of 10E8 helical epitope at the membrane interface

    Scientific Reports, Vol. 6

2015

  1. Fusion-competent state induced by a C-terminal HIV-1 fusion peptide in cholesterol-rich membranes

    Biochimica et Biophysica Acta - Biomembranes, Vol. 1848, Núm. 4, pp. 1014-1022

  2. The atomic structure of the HIV-1 gp41 transmembrane domain and its connection to the immunogenic membrane-proximal external region

    Journal of Biological Chemistry, Vol. 290, Núm. 21, pp. 12999-13015

  3. The use of liposomes to shape epitope structure and modulate immunogenic responses of peptide vaccines against HIV MPER

    Advances in Protein Chemistry and Structural Biology (Academic Press Inc.), pp. 15-54

2014

  1. Cholesterol-dependent membrane fusion induced by the gp41 membrane-proximal external region-transmembrane domain connection suggests a mechanism for broad HIV-1 neutralization

    Journal of Virology, Vol. 88, Núm. 22, pp. 13367-13377

  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

  3. The three lives of viral fusion peptides

    Chemistry and Physics of Lipids, Vol. 181, pp. 40-55

2012

  1. Mechanism of membrane perturbation by the HIV-1 gp41 membrane-proximal external region and its modulation by cholesterol

    Biochimica et Biophysica Acta - Biomembranes, Vol. 1818, Núm. 11, pp. 2521-2528

2011

  1. A new paradigm in molecular recognition? Specific antibody binding to membrane-inserted HIV-1 epitopes.

    Journal of molecular recognition : JMR, Vol. 24, Núm. 4, pp. 642-646

  2. Destabilization exerted by peptides derived from the membrane-proximal external region of HIV-1 gp41 in lipid vesicles supporting fluid phase coexistence

    Biochimica et Biophysica Acta - Biomembranes, Vol. 1808, Núm. 7, pp. 1797-1805

  3. Membrane-proximal external HIV-1 gp41 motif adapted for destabilizing the highly rigid viral envelope

    Biophysical Journal, Vol. 101, Núm. 10, pp. 2426-2435