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

A comparison of the ability of rilpivirine (TMC278) and selected analogues to inhibit clinically relevant HIV-1 reverse transcriptase mutants.

Retrovirology - 5 Dec 2012

Johnson Barry C, Pauly Gary T, Rai Ganesha, Patel Disha, Bauman Joseph D, Baker Heather L, Das Kalyan, Schneider Joel P, Maloney David J, Arnold Eddy, Thomas Craig J, Hughes Stephen H

Abstract excerpt

BACKGROUND: The recently approved anti-AIDS drug rilpivirine (TMC278, Edurant) is a nonnucleoside inhibitor (NNRTI) that binds to reverse transcriptase (RT) and allosterically blocks the chemical step of DNA synthesis. In contrast to earlier NNRTIs, rilpivirine retains potency against well-characterized, clinically relevant RT mutants. Many structural analogues of rilpivirine are described in the patent...

Read the complete abstract on PubMed

Topics

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

Share to Crystallography
Share to HIV Infections

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

Share to HIV Reverse Transcriptase

Share to Molecular Structure

Share to Nitriles

Share to Pyrimidines

Share to Reverse Transcriptase Inhibitors

Share to Rilpivirine

Source

Open in PubMed Open full text

Identifiers

PMID: 23217210
DOI: 10.1186/1742-4690-9-99
PMCID: PMC3549755

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

A comparison of the ability of rilpivirine (TMC278) and selected analogues to inhibit clinically relevant HIV-1 reverse transcriptase mutants.PMID 23217210Read ↗

Rilpivirine analogs potently inhibit drug-resistant HIV-1 mutants.Semantic proximity Read ↗

Structure-based non-nucleoside inhibitor design: Developing inhibitors that are effective against resistant mutants.Semantic proximity Read ↗

Development of enhanced HIV-1 non-nucleoside reverse transcriptase inhibitors with improved resistance and pharmacokinetic profiles.Semantic proximity Read ↗

Rilpivirine and Doravirine Have Complementary Efficacies Against NNRTI-Resistant HIV-1 Mutants.Semantic proximity Read ↗

The Current Status of the NNRTI Family of Antiretrovirals Used Against HIV InfectionSemantic proximity Read ↗

Looking for an Active Conformation of the Future HIV Type-1 Non-Nucleoside Reverse Transcriptase InhibitorsSemantic proximity Read ↗

Design of non-nucleoside inhibitors of HIV-1 reverse transcriptase with improved drug resistance properties. 1.Semantic proximity Read ↗

Structure-enhanced methods in the development of non-nucleoside inhibitors targeting HIV reverse transcriptase variants.Semantic proximity Read ↗

Lersivirine, a Nonnucleoside Reverse Transcriptase Inhibitor with Activity against Drug-Resistant Human Immunodeficiency Virus Type 1Semantic proximity Read ↗

Drug-like property-driven optimization of 4-substituted 1,5-diarylanilines as potent HIV-1 non-nucleoside reverse transcriptase inhibitors against rilpivirine-resistant mutant virus.Semantic proximity Read ↗

Crystal structures of HIV-1 reverse transcriptase with etravirine (TMC125) and rilpivirine (TMC278): implications for drug design.Semantic proximity Read ↗

Crystal engineering of HIV-1 reverse transcriptase for structure-based drug designSemantic proximity Read ↗

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