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Article

Identification of an amino acid substitution involved in the reduction of sensitivity of HIV-1 to an inhibitor of viral proteinase.

Acta virologica - 1 Oct 1994

Turriziani O, Antonelli G, Jacobsen H, Mous J, Riva E, Pistello M, Dianzani F

Abstract excerpt

Clones derived from HIV variants previously characterized as resistant to Ro31-8959, an inhibitor of viral proteinase (PR), were sequenced. Substitution of glycine by valine at position 48 of the PR protein was found. None of the 20 clones derived from wild type HTLV-IIIB contain this mutation. Since such a position is located in a conserved region of PR, it is possible that the substitution can affect the...

Topics

Base Sequence
DNA Primers
Drug Resistance, Microbial
Glycine
HIV
HIV Protease Inhibitors
HIV-1
Humans
Isoquinolines
Molecular Sequence Data
Mutation

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Quinolines

Saquinavir

Valine

Viral Proteins

Source

Identifiers

PMID: 7726006

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 29 Aug 2026. Prepared record publication-7726006-2026-08-29.1. Manifest publication-graph-cohort-2026-08-29.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 29 Aug 2026.

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