Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

In vitro selection and characterization of VX-478 resistant HIV-1 variants.

Advances in experimental medicine and biology - 1 Jan 1998

Pazhanisamy S, Partaledis J A, Rao B G, Livingston D J

Abstract excerpt

VX-478 (141W94), a potent inhibitor of HIV protease, is in late stage clinical trials for the treatment of HIV infection and AIDS. Resistant viruses were raised in vitro by passage of HIV-1IIIB in the presence of increasing concentrations of VX-478 and the related hydroxyethylamino sulfonamide inhibitor VB-11,328. By direct PCR analysis of selected viruses, a number of mutations were identified (L10F, M46I, I47V,...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Drug Resistance
Share to Genetic Variation
Share to HIV-1

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to HIV Protease

Share to HIV Protease Inhibitors

Share to Mutation

Share to Protein Conformation

Share to Sulfonamides

Source

Identifiers

PMID: 9561202
DOI: 10.1007/978-1-4615-5373-1_10

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

In vitro selection and characterization of VX-478 resistant HIV-1 variants.PMID 9561202Read ↗

Kinetic characterization of human immunodeficiency virus type-1 protease-resistant variants.Semantic proximity Read ↗

In vitro selection and characterization of human immunodeficiency virus type 1 (HIV-1) isolates with reduced sensitivity to hydroxyethylamino sulfonamide inhibitors of HIV-1 aspartyl proteaseSemantic proximity Read ↗

A mutation in human immunodeficiency virus type 1 protease at position 88, located outside the active site, confers resistance to the hydroxyethylurea inhibitor SC-55389A.Semantic proximity Read ↗

Characterization of a human immunodeficiency virus type 1 variant with reduced sensitivity to an aminodiol protease inhibitor.Semantic proximity Read ↗

Characterization of human immunodeficiency virus type 1 variants with increased resistance to a C2-symmetric protease inhibitor.Semantic proximity Read ↗

In vitro development of resistance to human immunodeficiency virus protease inhibitor GW640385.Semantic proximity Read ↗

In vitro selection and characterization of human immunodeficiency virus type 1 variants with increased resistance to ABT-378, a novel protease inhibitor.Semantic proximity Read ↗

Characterization of HIV-1 protease mutants: random, directed, selected.Semantic proximity Read ↗

Characterization of human immunodeficiency virus type 1 mutants with decreased sensitivity to proteinase inhibitor Ro 31-8959.Semantic proximity Read ↗

Rapid genetic selection of inhibitor-resistant protease mutants: clinically relevant and novel mutants of the HIV protease.Semantic proximity Read ↗

In vitro resistance studies of hepatitis C virus serine protease inhibitors, VX-950 and BILN 2061: structural analysis indicates different resistance mechanisms.Semantic proximity Read ↗

Three-dimensional Structure of a Mutant HIV-1 Protease Displaying Cross-resistance to All Protease Inhibitors in Clinical TrialsSemantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.