Conformational Modifications of gB from Herpes Simplex Virus Type 1 Analyzed by Synthetic Peptides (Articolo in rivista)

Type
Label
  • Conformational Modifications of gB from Herpes Simplex Virus Type 1 Analyzed by Synthetic Peptides (Articolo in rivista) (literal)
Anno
  • 2013-01-01T00:00:00+01:00 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi
  • 10.1021/jm400771k (literal)
Alternative label
  • Cantisani, Marco; Falanga, Annarita; Incoronato, Novella; Russo, Luigi; De Simone, Alfonso; Morelli, Giancarlo; Berisio, Rita; Galdiero, Massimiliano; Galdiero, Stefania (2013)
    Conformational Modifications of gB from Herpes Simplex Virus Type 1 Analyzed by Synthetic Peptides
    in Journal of medicinal chemistry
    (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
  • Cantisani, Marco; Falanga, Annarita; Incoronato, Novella; Russo, Luigi; De Simone, Alfonso; Morelli, Giancarlo; Berisio, Rita; Galdiero, Massimiliano; Galdiero, Stefania (literal)
Pagina inizio
  • 8366 (literal)
Pagina fine
  • 8376 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume
  • 56 (literal)
Rivista
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#pagineTotali
  • 11 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroFascicolo
  • 21 (literal)
Note
  • ISI Web of Science (WOS) (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni
  • University of Naples Federico II; University of Naples Federico II; University of Naples Federico II; Istituto Italiano di Tecnologia - IIT; Seconda Universita degli Studi di Napoli; Imperial College London; Consiglio Nazionale delle Ricerche (CNR) (literal)
Titolo
  • Conformational Modifications of gB from Herpes Simplex Virus Type 1 Analyzed by Synthetic Peptides (literal)
Abstract
  • Entry of enveloped viruses requires fusion of viral and cellular membranes, driven by conformational changes of viral glycoproteins. The crystallized trimeric glycoprotein gB of herpes simplex virus has been described as a postfusion conformation, and several studies prove that like other class III fusion proteins, gB undergoes a pH-dependent switch between the pre- and postfusion conformations. Using several biophysical techniques, we show that peptides corresponding to the long helix of the gB postfiision structure interfere with the membrane fusion event, likely hampering the conformational rearrangements from the pre- to the postfusion structures. Those peptides represent good candidates for further design of peptidomimetic antagonists capable of blocking the fusion process. (literal)
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