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

Understanding the effect of drug-resistant mutations of HIV-1 intasome on raltegravir action through molecular modeling study

20 Apr 2012

Abstract excerpt

Raltegravir is the first FDA-approved drug targeting the strand transfer step of HIV-1 integration. However, the rapid emergence of viral strains that are highly resistant to raltegravir has become a critical problem. Unfortunately, the detailed molecular mechanism of how HIV-1 integrase (IN) mutations actually confer drug resistance is not well understood. In the present study, starting from our previously...

Read the complete abstract on PubMed

Topics

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

Share to HIV/AIDS drug development and treatment
Share to HIV/AIDS Research and Interventions
Share to HIV Research and Treatment

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Source

Identifiers

PMID: 22648037
DOI: 10.1039/c2mb25114k

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 5 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Understanding the effect of drug-resistant mutations of HIV-1 intasome on raltegravir action through molecular modeling studyPMID 22648037Read ↗

Molecular mechanism of HIV‐1 integrase–vDNA interactions and strand transfer inhibitor action: A molecular modeling perspectiveSemantic proximity Read ↗

Impact of resistance mutations on inhibitor binding to HIV-1 integrase.Semantic proximity Read ↗

Molecular dynamic simulations to investigate the structural impact of known drug resistance mutations on HIV-1C Integrase-Dolutegravir binding.Semantic proximity Read ↗

Resistance to HIV-1 integrase inhibitors: A structural perspective.Semantic proximity Read ↗

Mechanisms of HIV-1 integrase resistance to dolutegravir and potent inhibition of drug-resistant variants.Semantic proximity Read ↗

Drug resistance mechanisms of three mutations V32I, I47V and V82I in HIV-1 protease toward inhibitors probed by molecular dynamics simulations and binding free energy predictionsSemantic proximity Read ↗

Some insights into mechanism for binding and drug resistance of wild type and I50V V82A and I84V mutations in HIV-1 protease with GRL-98065 inhibitor from molecular dynamic simulations.Semantic proximity Read ↗

Resistance to Integrase InhibitorsSemantic proximity Read ↗

Revealing the binding and drug resistance mechanism of amprenavir, indinavir, ritonavir, and nelfinavir complexed with HIV-1 protease due to double mutations G48T/L89M by molecular dynamics simulations and free energy analyses.Semantic proximity Read ↗

Exploring the drug resistance mechanism of active site, non-active site mutations and their cooperative effects in CRF01_AE HIV-1 protease: molecular dynamics simulations and free energy calculations.Semantic proximity Read ↗

Induced-fit docking approach provides insight into the binding mode and mechanism of action of HIV-1 integrase inhibitors.Semantic proximity Read ↗

HIV-1 IN alternative molecular recognition of DNA induced by raltegravir resistance mutations.Semantic proximity Read ↗

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