Now showing items 1-4 of 4

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      Functional organization of the HIV lipid envelope 

      Huarte Arrayago, Nerea; Carravilla Palomanes, Pablo ORCID; Cruz, Antonio; Lorizate Nogales, Maier; Nieto Garai, Jon Ander; Kräusslich, Hans-Georg; Pérez Gil, Jesús; Requejo Isidro, José; Nieva Escandón, José Luis (Nature, 2016-09-28)
      The chemical composition of the human immunodeficiency virus type 1 (HIV-1) membrane is critical for fusion and entry into target cells, suggesting that preservation of a functional lipid bilayer organization may be required ...
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      Pore-forming activity of pestivirus p7 in a minimal model system supports genus-specific viroporin function 

      Largo Pereda, Eneko; Gladue, Douglas P.; Huarte Arrayago, Nerea; Borca, Manuel V.; Nieva Escandón, José Luis (Elsevier, 2013-11-02)
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      Recognition of Membrane-Bound Fusion-Peptide/MPER Complexes by the HIV-1 Neutralizing 2F5 Antibody : Implications for Anti-2F5 Immunogenicity 

      Huarte Arrayago, Nerea; Araujo Pasarín, Aitziber; Arranz, Rocio; Lorizate Nogales, Maier; Quendler, Heribert; Kunert, Renate; Valpuesta, José M.; Nieva Escandón, José Luis (Public Library of Science, 2012-12-21)
      The membrane proximal external region (MPER) of the fusogenic HIV-1 glycoprotein-41 harbors the epitope sequence recognized by 2F5, a broadly neutralizing antibody isolated from an infected individual. Structural mimicry ...
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      The three lives of viral fusion peptides 

      Apellaniz Unzalu, Beatriz ORCID; Huarte Arrayago, Nerea; Largo Pereda, Eneko; Nieva Escandón, José Luis (Elsevier, 2014-04)
      Fusion peptides comprise conserved hydrophobic domains absolutely required for the fusogenic activity of glycoproteins from divergent virus families. After 30 years of intensive research efforts, the structures and functions ...