The Epstein-Barr virus LMP1 cytoplasmic carboxy terminus is essential for B-lymphocyte transformation; fibroblast cocultivation complements a critical function within the terminal 155 residues.

Similar Items

• Epstein-Barr virus recombinant molecular genetic analysis of the LMP1 amino-terminal cytoplasmic domain reveals a probable structural role, with no component essential for primary B-lymphocyte growth transformation.
  od: Izumi, K M, i dr.
  Izdano: (1994)
• Association of TRAF1, TRAF2, and TRAF3 with an Epstein-Barr virus LMP1 domain important for B-lymphocyte transformation: role in NF-kappaB activation.
  od: Devergne, O, i dr.
  Izdano: (1996)
• The last seven transmembrane and carboxy-terminal cytoplasmic domains of Epstein-Barr virus latent membrane protein 2 (LMP2) are dispensable for lymphocyte infection and growth transformation in vitro.
  od: Longnecker, R, i dr.
  Izdano: (1993)
• The Epstein–Barr virus LMP1 amino acid sequence that engages tumor necrosis factor receptor associated factors is critical for primary B lymphocyte growth transformation
  od: Izumi, Kenneth M., i dr.
  Izdano: (1997)
• A second Epstein-Barr virus membrane protein (LMP2) is expressed in latent infection and colocalizes with LMP1.
  od: Longnecker, R, i dr.
  Izdano: (1990)