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

Adaptive inhibitors of the HIV-1 protease.

Progress in biophysics and molecular biology - 1 Jun 2005

Ohtaka Hiroyasu, Freire Ernesto

Abstract excerpt

A significant obstacle to the efficacy of drugs directed against viral targets is the presence of amino acid polymorphisms in the targeted molecules. Amino acid polymorphisms may occur naturally due to the existence of variations within and between viral strains or as the result of mutations associated with drug resistance. An ideal drug will be one that is extremely effective against a primary target and...

Read the complete abstract on PubMed

Topics

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

Share to Acquired Immunodeficiency Syndrome
Share to Anti-HIV Agents
Share to Drug Delivery Systems

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Drug Design

Share to Drug Resistance, Multiple, Viral

Share to Gene Expression Regulation, Viral

Share to HIV Protease

Share to HIV Protease Inhibitors

Source

Identifiers

PMID: 15572155
DOI: 10.1016/j.pbiomolbio.2004.07.005

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Adaptive inhibitors of the HIV-1 protease.PMID 15572155Read ↗

Incorporating target heterogeneity in drug design.Semantic proximity Read ↗

Thermodynamic rules for the design of high affinity HIV-1 protease inhibitors with adaptability to mutations and high selectivity towards unwanted targets.Semantic proximity Read ↗

Structural and Thermodynamic Basis of Resistance to HIV-1 Protease Inhibition: Implications for Inhibitor DesignSemantic proximity Read ↗

“Old Dogs with New Tricks”: exploiting alternative mechanisms of action and new drug design strategies for clinically validated HIV targetsSemantic proximity Read ↗

Elasticity-Associated Functionality and Inhibition of the HIV Protease.Semantic proximity Read ↗

A structural and thermodynamic escape mechanism from a drug resistant mutation of the HIV-1 protease.Semantic proximity Read ↗

Slow-, tight-binding HIV-1 reverse transcriptase non-nucleoside inhibitors highly active against drug-resistant mutants.Semantic proximity Read ↗

Non-active site mutations in the HIV protease: Diminished drug binding affinity is achieved through modulating the hydrophobic sliding mechanism.Semantic proximity Read ↗

Unusual binding mode of an HIV-1 protease inhibitor explains its potency against multi-drug-resistant virus strains.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 resistance: lessons from HIV-1 protease.Semantic proximity Read ↗

Design of mutation-resistant HIV protease inhibitors with the substrate envelope hypothesis.Semantic proximity Read ↗

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