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

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

Journal of virology - 1 May 2007

Muzammil S, Armstrong A A, Kang L W, Jakalian A, Bonneau P R, Schmelmer V, Amzel L M, Freire E

Abstract excerpt

Drug resistance is a major problem affecting the clinical efficacy of antiretroviral agents, including protease inhibitors, in the treatment of infection with human immunodeficiency virus type 1 (HIV-1)/AIDS. Consequently, the elucidation of the mechanisms by which HIV-1 protease inhibitors maint...

Read the complete abstract on PubMed

Topics

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

Share to Crystallography, X-Ray
Share to HIV Protease
Share to HIV Protease Inhibitors

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Hydrogen Bonding

Share to Molecular Structure

Share to Pyridines

Share to Pyrones

Share to Sulfonamides

Source

Open in PubMed Open full text

Identifiers

PMID: 17360759
DOI: 10.1128/JVI.02706-06
PMCID: PMC1900215

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 2 Sept 2026. Prepared record publication-17360759-2026-09-02.2. 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

Unique thermodynamic response of tipranavir to human immunodeficiency virus type 1 protease drug resistance mutations.PMID 17360759Read ↗

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

A contribution to the drug resistance mechanism of darunavir, amprenavir, indinavir, and saquinavir complexes with HIV-1 protease due to flap mutation I50V: a systematic MM-PBSA and thermodynamic integration study.Semantic proximity Read ↗

Genotypic changes in human immunodeficiency virus type 1 protease associated with reduced susceptibility and virologic response to the protease inhibitor tipranavir.Semantic proximity Read ↗

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

An inhibitor-interaction intermediate of HIV-1 protease, revealed by Isothermal Titration Calorimetry and NMR spectroscopySemantic proximity Read ↗

Energetic basis for drug resistance of HIV-1 protease mutants against amprenavir.Semantic proximity Read ↗

Tipranavir: a new protease inhibitor for the treatment of antiretroviral-experienced HIV-infected patients.Semantic proximity Read ↗

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

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

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

Extreme multidrug resistant HIV-1 protease with 20 mutations is resistant to novel protease inhibitors with P1'-pyrrolidinone or P2-tris-tetrahydrofuran.Semantic proximity Read ↗

A synergy of activity, stability, and inhibitor-interaction of HIV-1 protease mutants evolved under drug-pressure.Semantic proximity Read ↗

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