Document 0004
 DOCN  M9480004
 TI    Sensitivity of (138 Glu-->Lys) mutated human immunodeficiency virus type
       1 (HIV-1) reverse transcriptase (RT) to HIV-1-specific RT inhibitors.
 DT    9410
 AU    Balzarini J; Kleim JP; Riess G; Camarasa MJ; De Clercq E; Karlsson A;
       Rega Institute for Medical Research, Katholieke Universiteit; Leuven,
       Belgium.
 SO    Biochem Biophys Res Commun. 1994 Jun 30;201(3):1305-12. Unique
       Identifier : AIDSLINE MED/94296403
 AB    Human immunodeficiency virus type 1 (HIV-1) recombinant reverse
       transcriptase (RT) containing lysine (Lys) instead of glutamic acid
       (Glu) at position 138 proved fully resistant to the inhibitory effect of
       TSAO derivatives, but retained marked sensitivity to all other
       HIV-1-specific inhibitors investigated. In contrast, 181 Tyr-->Cys
       mutated RT lost sensitivity to all HIV-1-specific inhibitors. There was
       a close correlation between the sensitivity/resistance pattern of
       HIV-1-specific inhibitors against mutated (138 Glu-->Lys) recombinant
       HIV-1 RT and mutant virus strains selected for resistance against
       TSAO-m3T in cell culture and proven to contain the 138-Lys mutation as
       the sole mutation within the amino acid 50-270 region of their RT.
 DE    *Antiviral Agents  Drug Resistance, Microbial  Glutamates/CHEMISTRY
       Human  HIV-1/*DRUG EFFECTS/ENZYMOLOGY  Mutagenesis, Site-Directed
       Pyridones/PHARMACOLOGY  Recombinant Proteins  Reverse
       Transcriptase/*ANTAGONISTS & INHIB/CHEMISTRY  Structure-Activity
       Relationship  Support, Non-U.S. Gov't  Thymidine/ANALOGS &
       DERIVATIVES/CHEMISTRY/PHARMACOLOGY  JOURNAL ARTICLE

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