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M9460193.TXT
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1994-06-12
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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).