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

An allosteric modulator of HIV-1 protease shows equipotent inhibition of wild-type and drug-resistant proteases.

Journal of medicinal chemistry - 14 Aug 2014

Ung Peter M-U, Dunbar James B, Gestwicki Jason E, Carlson Heather A

Abstract excerpt

NMR and MD simulations have demonstrated that the flaps of HIV-1 protease (HIV-1p) adopt a range of conformations that are coupled with its enzymatic activity. Previously, a model was created for an allosteric site located between the flap and the core of HIV-1p, called the Eye site (Biopolymers 2008, 89, 643-652). Here, results from our first study were combined with a ligand-based, lead-hopping method to...

Read the complete abstract on PubMed

Topics

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

Share to Allosteric Regulation
Share to Allosteric Site

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Benzothiazoles

Share to Drug Resistance, Multiple, Viral

Share to HIV Protease

Share to HIV Protease Inhibitors

Share to Phthalimides

Share to Small Molecule Libraries

Source

Open in PubMed Open full text

Identifiers

PMID: 25062388
DOI: 10.1021/jm5008352
PMCID: PMC4136727

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

An allosteric modulator of HIV-1 protease shows equipotent inhibition of wild-type and drug-resistant proteases.PMID 25062388Read ↗

Molecular docking-based screening for novel inhibitors of the human immunodeficiency virus type 1 protease that effectively reduce the viral replication in human cellsSemantic proximity Read ↗

Contrasting the effect of hinge region insertions and non-active site mutations on HIV protease-inhibitor interactions: Insights from altered flap dynamics.Semantic proximity Read ↗

Differential Flap Dynamics in Wild-Type and a Drug Resistant Variant of HIV-1 Protease Revealed by Molecular Dynamics and NMR RelaxationSemantic proximity Read ↗

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

Flap-site Fragment Restores Back Wild-type Behaviour in Resistant Form of HIV Protease.Semantic proximity Read ↗

Challenges and approaches in the discovery of human immunodeficiency virus type‐1 non‐nucleoside reverse transcriptase inhibitorsSemantic proximity Read ↗

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

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

Drug pressure selected mutations in HIV-1 protease alter flap conformations.Semantic proximity Read ↗

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

Evolution of drug resistance drives progressive destabilizations in functionally conserved molecular dynamics of the flap region of the HIV-1 proteaseSemantic proximity Read ↗

Dynamical Network of HIV-1 Protease Mutants Reveals the Mechanism of Drug Resistance and Unhindered Activity.Semantic proximity Read ↗

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