Mutation of a conserved residue (D123) required for oligomerization of human immunodeficiency virus type 1 Nef protein abolishes interaction with human thioesterase and results in impairment of Nef biological functions.

@article{Liu2000MutationOA,
  title={Mutation of a conserved residue (D123) required for oligomerization of human immunodeficiency virus type 1 Nef protein abolishes interaction with human thioesterase and results in impairment of Nef biological functions.},
  author={Lang Xia Liu and Nikolaus Heveker and Oliver T. Fackler and Stefan Arold and Sylvie Le Gall and Katy Janvier and Boris Matija Peterlin and Christian Dumas and Olivier Schwartz and Serge B{\'e}nichou and Richard Benarous},
  journal={Journal of virology},
  year={2000},
  volume={74 11},
  pages={5310-9}
}
Nef is a myristoylated protein of 27 to 35 kDa that is conserved in primate lentiviruses. In vivo, Nef is required for high viral load and full pathological effects. In vitro, Nef has at least four activities: induction of CD4 and major histocompatibility complex (MHC) class I downregulation, enhancement of viral infectivity, and alteration of T-cell activation pathways. We previously reported that the Nef protein from human immunodeficiency virus type 1 interacts with a novel human… CONTINUE READING
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