Document 0193
 DOCN  M9460193
 TI    Regulation of human immunodeficiency virus Nef protein by
       phosphorylation.
 DT    9408
 AU    Bandres JC; Luria S; Ratner L; Department of Medicine, Washington
       University School of Medicine,; St. Louis, Missouri.
 SO    Virology. 1994 May 15;201(1):157-61. Unique Identifier : AIDSLINE
       MED/94233766
 AB    Human immunodeficiency virus isolates express a Nef protein with either
       an alanine or a threonine at amino acid residue 15. The threonine
       residue is a site for phosphorylation by protein kinase C. Jurkat T
       cells constitutively expressing the alanine variant of Nef exhibit the
       ability to downregulate the induction of transcription factors NF-kB and
       AP-1. In contrast, Jurkat cells with the threonine variant of Nef are at
       least partially restored in their ability to recruit NF-kB and AP-1.
 DE    Binding Sites  Down-Regulation (Physiology)  DNA, Viral/METABOLISM
       Electrophoresis, Polyacrylamide Gel/METHODS  Gene Products,
       nef/ANALYSIS/*CHEMISTRY/*PHYSIOLOGY  Genes, nef/GENETICS  Human
       HIV/CHEMISTRY/*METABOLISM  HIV Long Terminal Repeat/GENETICS
       Interleukin-2/GENETICS  NF-kappa B/*BIOSYNTHESIS  Phosphorylation  Point
       Mutation  Promoter Regions (Genetics)/GENETICS  Proto-Oncogene Proteins
       c-jun/*BIOSYNTHESIS  Support, Non-U.S. Gov't  Support, U.S. Gov't,
       Non-P.H.S.  Threonine/METABOLISM  Transcription, Genetic  Tumor Cells,
       Cultured  JOURNAL ARTICLE

       SOURCE: National Library of Medicine.  NOTICE: This material may be
       protected by Copyright Law (Title 17, U.S.Code).