Publikationen, an denen er mitarbeitet José Luis Nieva Escandon (21)

2017

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

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

  2. Structure-Related Roles for the Conservation of the HIV-1 Fusion Peptide Sequence Revealed by Nuclear Magnetic Resonance

    Biochemistry, Vol. 56, Núm. 41, pp. 5503-5511

2016

  1. Functional organization of the HIV lipid envelope

    Scientific Reports, Vol. 6

2015

  1. Two-photon laurdan studies of the ternary lipid mixture DOPC:SM:Cholesterol reveal a single liquid phase at sphingomyelin:cholesterol ratios lower than 1

    Langmuir, Vol. 31, Núm. 9, pp. 2808-2817

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. Pore-forming activity of pestivirus p7 in a minimal model system supports genus-specific viroporin function

    Antiviral Research, Vol. 101, Núm. 1, pp. 30-36

  3. 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

  4. The three lives of viral fusion peptides

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

2012

  1. Recognition of Membrane-Bound Fusion-Peptide/MPER Complexes by the HIV-1 Neutralizing 2F5 Antibody: Implications for Anti-2F5 Immunogenicity

    PLoS ONE, Vol. 7, Núm. 12

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. 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

  3. Membrane-Transferring Regions of gp41 as Targets for HIV-1 Fusion Inhibition and Viral Neutralization

    Current Topics in Medicinal Chemistry, Vol. 11, Núm. 24, pp. 2985-2996

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

  2. Confocal microscopy of giant vesicles supports the absence of HIV-1 neutralizing 2F5 antibody reactivity to plasma membrane phospholipids

    FEBS Letters, Vol. 584, Núm. 8, pp. 1591-1596

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. Functional and structural characterization of 2B viroporin membranolytic domains

    Biochemistry, Vol. 47, Núm. 40, pp. 10731-10739

  2. Interfacial pre-transmembrane domains in viral proteins promoting membrane fusion and fission

    Biochimica et Biophysica Acta - Biomembranes, Vol. 1778, Núm. 7-8, pp. 1624-1639

  3. The broadly neutralizing anti-human immunodeficiency virus type 1 4E10 monoclonal antibody is better adapted to membrane-bound epitope recognition and blocking than 2F5

    Journal of Virology, Vol. 82, Núm. 18, pp. 8986-8996

2006

  1. Hexapeptides that interfere with HIV-1 fusion peptide activity in liposomes block GP41-mediated membrane fusion

    FEBS Letters, Vol. 580, Núm. 11, pp. 2561-2566

  2. Recognition and blocking of HIV-1 gp41 pre-transmembrane sequence by monoclonal 4E10 antibody in a raft-like membrane environment

    Journal of Biological Chemistry, Vol. 281, Núm. 51, pp. 39598-39606