Selected article for: "amino acid and carboxyl terminus"

Author: Wodrich, Harald; Henaff, Daniel; Jammart, Baptist; Segura-Morales, Carolina; Seelmeir, Sigrid; Coux, Olivier; Ruzsics, Zsolt; Wiethoff, Christopher M.; Kremer, Eric J.
Title: A Capsid-Encoded PPxY-Motif Facilitates Adenovirus Entry
  • Document date: 2010_3_19
  • ID: 1mjmttec_3
    Snippet: A role for the ubiquitylation machinery during egress of enveloped viruses is better understood. Egress involves the transport of assembled capsids, subviral structures or individual capsid proteins to assembly and budding sites at the cell surface or at intracellular membranes [1] . Budding, and potentially trafficking, to the egress site requires an intact class E vesicular sorting pathway (VSP, [13, 14] . The VSP is believed to involve the con.....
    Document: A role for the ubiquitylation machinery during egress of enveloped viruses is better understood. Egress involves the transport of assembled capsids, subviral structures or individual capsid proteins to assembly and budding sites at the cell surface or at intracellular membranes [1] . Budding, and potentially trafficking, to the egress site requires an intact class E vesicular sorting pathway (VSP, [13, 14] . The VSP is believed to involve the consecutive activity of three distinct heteromeric complexes termed endosomal sorting complexes required for transport (ESCRT-I, -II and -III, [15] ). The capsid proteins of several enveloped viruses encode 'late domains' that specifically interact with ESCRT components and redirect them towards the site of viral egress [13] . Some late domains of the PPxY motif type (where x can be any amino acid) require the binding of ubiquitin ligases of the Nedd4 family of HECT-E3 ubiquitin ligases (Homologous to E6-AP Carboxyl Terminus) for efficient ESCRT recruitment [13] .

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