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 Thermodynamic Basis of Resistance to HIV-1 Protease Inhibition: Implications for Inhibitor Design

1 Dec 2003

Abstract excerpt

One of the most serious side effects associated with the therapy of HIV-1 infection is the appearance of viral strains that exhibit resistance to protease inhibitors. At the molecular level, resistance to protease inhibition predominantly takes the form of mutations within the protease molecule that preferentially lower the affinity of protease inhibitors with respect to protease substrates, while still...

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 Research and Treatment
Share to Pneumocystis jirovecii pneumonia detection and treatment

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Source

Identifiers

PMID: 14754432
DOI: 10.2174/1568005033481051

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Structural and Thermodynamic Basis of Resistance to HIV-1 Protease Inhibition: Implications for Inhibitor DesignPMID 14754432Read ↗

HIV-1 Protease: Structural Perspectives on Drug ResistanceSemantic 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 ↗

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

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

Structural Aspects of Drug Resistance and Inhibition of HIV-1 Reverse TranscriptaseSemantic proximity Read ↗

Unique thermodynamic response of tipranavir to human immunodeficiency virus type 1 protease drug resistance mutations.Semantic proximity Read ↗

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

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

Structure-based thermodynamic analysis of HIV-1 protease inhibitors.Semantic proximity Read ↗

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

Combating susceptibility to drug resistance: lessons from HIV-1 protease.Semantic proximity Read ↗

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