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

Structure-based thermodynamic analysis of HIV-1 protease inhibitors.

Biochemistry - 3 Jun 1997

Bardi J S, Luque I, Freire E

Abstract excerpt

A structural parametrization of the binding and folding energetics previously developed in this laboratory accounts quantitatively for the binding of 13 HIV-1 protease inhibitors for which high-resolution structures are available (A77003, A78791, A76928, A74704, A76889, VX478, SB203386, SB203238, SB206343, U100313, U89360, A98881, CGP53820). The binding free energies for the inhibitors are predicted with a...

Read the complete abstract on PubMed

Topics

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

Share to Binding Sites
Share to HIV Protease
Share to HIV Protease Inhibitors

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Models, Molecular

Share to Molecular Structure

Share to Mutation

Share to Protein Binding

Share to Thermodynamics

Source

Identifiers

PMID: 9184138
DOI: 10.1021/bi9701742

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

Structure-based thermodynamic analysis of HIV-1 protease inhibitors.PMID 9184138Read ↗

The binding energetics of first- and second-generation HIV-1 protease inhibitors: implications for drug design.Semantic proximity Read ↗

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

Automated molecular simulation based binding affinity calculator for ligand-bound HIV-1 proteases.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 ↗

How Mutations Can Resist Drug Binding yet Keep HIV-1 Protease Functional.Semantic proximity Read ↗

Prediction of HIV-1 protease/inhibitor affinity using RosettaLigand.Semantic proximity Read ↗

Extreme entropy-enthalpy compensation in a drug-resistant variant of HIV-1 protease.Semantic proximity Read ↗

Predicting structural effects in HIV-1 protease mutant complexes with flexible ligand docking and protein side-chain optimization.Semantic proximity Read ↗

Computational study of protein specificity: the molecular basis of HIV-1 protease drug resistance.Semantic proximity Read ↗

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

Automated On-the-Fly Optimization of Resource Allocation for Efficient Free Energy Simulations.Semantic proximity Read ↗

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

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