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

Drug resistance-associated mutations in Plasmodium UBP-1 disrupt its essential deubiquitinating activity.

The Journal of biological chemistry - 1 Mar 2025

Smith Cameron J, Eavis Heledd, Briggs Carla, Henrici Ryan, Karpiyevich Maryia, Ansbro Megan R, Hoshizaki Johanna, van der Heden van Noort Gerbrand J, Ascher David B, Sutherland Colin J, Lee Marcus C S, Artavanis-Tsakonas Katerina

Abstract excerpt

Deubiquitinating enzymes function to cleave ubiquitin (Ub) moieties from modified proteins, serving to maintain the pool of free Ub in the cell while simultaneously impacting the fate and function of a target protein. Like all eukaryotes, Plasmodium parasites rely on the dynamic addition and removal of Ub for their own growth and survival. While humans possess around 100 deubiquitinases, Plasmodium contains ∼20...

Read the complete abstract on PubMed

Topics

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

Share to Antimalarials
Share to Drug Resistance

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Endocytosis

Share to Plasmodium falciparum

Share to Point Mutation

Share to Protozoan Proteins

Share to Ubiquitin

Share to Ubiquitination

Source

Open in PubMed Open full text

Identifiers

PMID: 39909372
DOI: 10.1016/j.jbc.2025.108266
PMCID: PMC11927682

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 2 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Drug resistance-associated mutations in Plasmodium UBP-1 disrupt its essential deubiquitinating activity.PMID 39909372Read ↗

Drug resistance-associated mutations in <i>Plasmodium</i> UBP-1 disrupt ubiquitin hydrolysisSemantic proximity Read ↗

Targeting the Plasmodium Ubiquitin/Proteasome System with Anti- Malarial Compounds: Promises for the FutureSemantic proximity Read ↗

Mammalian deubiquitinating enzyme inhibitors display <i>in vitro</i> and <i>in vivo</i> activity against malaria parasites and potentiate artemisinin actionSemantic proximity Read ↗

Protein ubiquitylation is essential for the schizont to merozoite transition in <i>Plasmodium falciparum</i> blood-stage developmentSemantic proximity Read ↗

The Skp1-Cullin1-FBXO1 complex is a pleiotropic regulator required for the formation of gametes and motile forms in Plasmodium bergheiSemantic proximity Read ↗

Unraveling the Ubiquitome of the Human Malaria ParasiteSemantic proximity Read ↗

Nedd8 hydrolysis by UCH proteases in Plasmodium parasitesSemantic proximity Read ↗

Experimentally Engineered Mutations in a Ubiquitin Hydrolase, UBP-1, Modulate In Vivo Susceptibility to Artemisinin and Chloroquine in Plasmodium berghei.Semantic proximity Read ↗

Enhanced cell stress response and protein degradation capacity underlie artemisinin resistance in Plasmodium falciparum.Semantic proximity Read ↗

Understanding the role of RBR-E3 ligase in regulation of cellular homeostasis in human malaria parasiteSemantic proximity Read ↗

The newly discovered role of endocytosis in artemisinin resistance.Semantic proximity Read ↗

Ubiquitin-Like Modifiers: Emerging Regulators of Protozoan ParasitesSemantic proximity Read ↗

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