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

Selection of HIV-1 for resistance to fifth-generation protease inhibitors reveals two independent pathways to high-level resistance.

eLife - 15 Mar 2023

Spielvogel Ean, Lee Sook-Kyung, Zhou Shuntai, Lockbaum Gordon J, Henes Mina, Sondgeroth Amy, Kosovrasti Klajdi, Nalivaika Ellen A, Ali Akbar, Yilmaz Nese Kurt, Schiffer Celia A, Swanstrom Ronald

Abstract excerpt

Darunavir (DRV) is exceptional among potent HIV-1 protease inhibitors (PIs) in high drug concentrations that are achieved in vivo. Little is known about the de novo resistance pathway for DRV. We selected for resistance to high drug concentrations against 10 PIs and their structural precursor DRV. Mutations accumulated through two pathways (anchored by protease mutations I50V or I84V). Small changes in the...

Read the complete abstract on PubMed

Topics

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

Share to Darunavir
Share to Drug Resistance, Viral

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to HIV Infections

Share to HIV Protease Inhibitors

Share to Mutation

Source

Open in PubMed Open full text

Identifiers

PMID: 36920025
DOI: 10.7554/eLife.80328
PMCID: PMC10065791

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 1 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Selection of HIV-1 for resistance to fifth-generation protease inhibitors reveals two independent pathways to high-level resistance.PMID 36920025Read ↗

In vitro selection of highly darunavir-resistant and replication-competent HIV-1 variants by using a mixture of clinical HIV-1 isolates resistant to multiple conventional protease inhibitors.Semantic proximity Read ↗

TMC310911, a novel human immunodeficiency virus type 1 protease inhibitor, shows in vitro an improved resistance profile and higher genetic barrier to resistance compared with current protease inhibitors.Semantic proximity Read ↗

In Vivo Emergence of a Novel Protease Inhibitor Resistance Signature in HIV-1 Matrix.Semantic proximity Read ↗

Drug resistance conferred by mutations outside the active site through alterations in the dynamic and structural ensemble of HIV-1 protease.Semantic proximity Read ↗

The impact of individual human immunodeficiency virus type 1 protease mutations on drug susceptibility is highly influenced by complex interactions with the background protease sequence.Semantic proximity Read ↗

Selection of high-level resistance to human immunodeficiency virus type 1 protease inhibitors.Semantic proximity Read ↗

In vitro and structural evaluation of PL-100 as a potential second-generation HIV-1 protease inhibitor.Semantic proximity Read ↗

Computational Prediction of HIV-1 Resistance to Protease Inhibitors.Semantic proximity Read ↗

Highly drug-resistant HIV-1 protease reveals decreased intra-subunit interactions due to clusters of mutations.Semantic proximity Read ↗

Combating Susceptibility to Drug ResistanceLessons from HIV-1 ProteaseSemantic proximity Read ↗

Evaluating the potency of HIV-1 protease drugs to combat resistance.Semantic proximity Read ↗

Combating susceptibility to drug resistance: lessons from HIV-1 protease.Semantic proximity Read ↗

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