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

Structural and energetic analyses of the effects of the K103N mutation of HIV-1 reverse transcriptase on efavirenz analogues.

Journal of medicinal chemistry - 22 Apr 2004

Udier-Blagović Marina, Tirado-Rives Julian, Jorgensen William L

Abstract excerpt

The effect of the K103N mutation of HIV-1 reverse transcriptase (RT) on the activity of efavirenz analogues was studied via Monte Carlo/free energy perturbation calculations. The relative fold resistance energies indicate that efavirenz binds to K103N RT in a manner similar to the wild-type enzym...

Read the complete abstract on PubMed

Topics

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

Share to Alkynes
Share to Benzoxazines
Share to Cyclopropanes

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to HIV Reverse Transcriptase

Share to Monte Carlo Method

Share to Oxazines

Share to Reverse Transcriptase Inhibitors

Share to Thermodynamics

Source

Identifiers

PMID: 15084137
DOI: 10.1021/jm0303507

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 2 Sept 2026. Prepared record publication-15084137-2026-09-02.2. Manifest publication-graph-cohort-2026-09-02.2.

Source receipt: PubMed via Helena Literature Corpus, retrieved 2 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Structural and energetic analyses of the effects of the K103N mutation of HIV-1 reverse transcriptase on efavirenz analogues.PMID 15084137Read ↗

Activity predictions for efavirenz analogues with the K103N mutant of HIV reverse transcriptase.Semantic proximity Read ↗

Antiviral drug design: computational analyses of the effects of the L100I mutation for HIV-RT on the binding of NNRTIs.Semantic proximity Read ↗

Structural basis for the inhibitory efficacy of efavirenz (DMP-266), MSC194 and PNU142721 towards the HIV-1 RT K103N mutant.Semantic proximity Read ↗

Understanding the basis of resistance in the irksome Lys103Asn HIV-1 reverse transcriptase mutant through targeted molecular dynamics simulations.Semantic proximity Read ↗

Energetics of mutation-induced changes in potency of lersivirine against HIV-1 reverse transcriptase.Semantic proximity Read ↗

Exploiting the hydrophobic channel of the NNIBP: Discovery of novel diarylpyrimidines as HIV-1 NNRTIs against wild-type and K103N mutant viruses.Semantic proximity Read ↗

Hybrid QM/MM Free-Energy Evaluation of Drug-Resistant Mutational Effect on the Binding of an Inhibitor Indinavir to HIV-1 Protease.Semantic proximity Read ↗

Novel theoretically designed HIV-1 non-nucleoside reverse transcriptase inhibitors derived from nevirapine.Semantic proximity Read ↗

Theoretical studies on the molecular basis of HIV-1RT/NNRTIs interactions.Semantic proximity Read ↗

Structural basis for the resilience of efavirenz (DMP-266) to drug resistance mutations in HIV-1 reverse transcriptase.Semantic proximity Read ↗

Monte Carlo calculations on HIV-1 reverse transcriptase complexed with the non-nucleoside inhibitor 8-Cl TIBO: contribution of the L100I and Y181C variants to protein stability and biological activity.Semantic proximity Read ↗

Molecular dynamics and Monte Carlo simulations for protein-ligand binding and inhibitor design.Semantic proximity Read ↗

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