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

Mutational scan of self-cleavage by HIV-1 protease provides new views of a conformationally dynamic mechanism.

Journal of virology - 21 Apr 2026

Nachum Gily S, Boucher Jeffrey I, Flynn Julia M, Quansah Princess, Nachum Sivan, Bolon Daniel N A

Abstract excerpt

The mechanism of conformationally dynamic proteins remains understudied because they are difficult to analyze structurally. For HIV-1 protease, the mechanism of cleavage by mature protease is well understood in large part because it forms a stable structure that is amenable to x-ray crystallography. However, self-cleavage or autoproteolysis of protease from the viral polyprotein involves transiently populated...

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-1

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to HIV Protease

Share to Models, Molecular

Share to Mutation

Share to Protein Conformation

Share to Proteolysis

Source

Open in PubMed Open full text

Identifiers

PMID: 41914756
DOI: 10.1128/jvi.02229-25
PMCID: PMC13098228

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 3 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Mutational scan of self-cleavage by HIV-1 protease provides new views of a conformationally dynamic mechanism.PMID 41914756Read ↗

Comprehensive fitness landscape of SARS-CoV-2 M <sup>pro</sup> reveals insights into viral resistance mechanismsSemantic proximity Read ↗

Regulation of autoproteolysis of the HIV-1 and HIV-2 proteases with engineered amino acid substitutionsSemantic proximity Read ↗

Mutations Proximal to Sites of Autoproteolysis and the α-Helix That Co-evolve under Drug Pressure Modulate the Autoprocessing and Vitality of HIV-1 Protease.Semantic proximity Read ↗

Studies of the autoprocessing of the HIV-1 protease using cleavage site mutants.Semantic proximity Read ↗

Hydrophobic core flexibility modulates enzyme activity in HIV-1 protease.Semantic proximity Read ↗

Exploring the interplay of stability and function in protein evolution: new methods further elucidate why protein stability is necessarily so tenuous and stability-increasing mutations compromise biological function.Semantic proximity Read ↗

Tobacco etch virus protease: mechanism of autolysis and rational design of stable mutants with wild-type catalytic proficiency.Semantic proximity Read ↗

Following autolysis in proteases by NMR: insights into multiple unfolding pathways and mutational plasticities.Semantic proximity Read ↗

Mutation of Asn-475 in the Venezuelan Equine Encephalitis Virus nsP2 Cysteine Protease Leads to a Self-Inhibited State.Semantic proximity Read ↗

Natural Occurring Polymorphisms in HIV-1 Integrase and RNase H Regulate Viral Release and Autoprocessing.Semantic proximity Read ↗

Large Scale Mutational and Kinetic Analysis of a Self-Hydrolyzing Deoxyribozyme.Semantic proximity Read ↗

The Impact of Gag Non-Cleavage Site Mutations on HIV-1 Viral Fitness from Integrative Modelling and SimulationsSemantic proximity Read ↗

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