ArticleNature chemical biology2019
ABHD10 is an S-depalmitoylase affecting redox homeostasis through peroxiredoxin-5.
Article in Nature chemical biology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 82 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
82 citing papers in PubMed, 127 citations in OpenAlex.
- The role of protein palmitoylation in disease pathogenesis and therapeutic innovation.Annals of medicine · 2026Review
- Emerging roles of α/β hydrolase domain (ABHD) proteins in S-palmitoylation modification: molecular mechanisms, structural features, and pathological implications.Cellular & molecular biology letters · 2026Review
- Proteome-Wide Analysis of Palmitoylated Proteins in Macrophages Reveals Novel Insights Into Early Immune Signaling.Proteomics · 2026Article
- Palmitoylation-related gene signature for immune subtyping, prognostic stratification, and immunotherapy guidance in hepatocellular carcinoma.Translational cancer research · 2026Article
- Long-Chain S-Acylation Is a Key Modulator During the Macrophage Inflammatory Response.Molecular & cellular proteomics : MCP · 2026Article
- Review
- A chemoproteomic atlas of the human purine interactome for regioselective ligand discovery.Nature communications · 2026Article
- ProteinJournal of pharmaceutical analysis · 2026Review
- Chemical Proteomics Identifies Ketogenesis-Mediated Cysteine Modifications Regulating Redox Function.Angewandte Chemie (International ed. in English) · 2026Article
- Multi-Omics Characterization of ABHD12 Across Pan-Cancer and Validation of Its Role in Promoting Proliferation and Metastasis in Breast Cancer.Breast cancer (Dove Medical Press) · 2026Article
- The Roles of ProteinCancer communications (London, England) · 2026Review
- Identification of the Antioxidant Enzyme B166 as a Novel Biomarker for Patients With Glioblastoma Multiforme.Analytical cellular pathology (Amsterdam) · 2026Article
- Epigenome-wide association study of nuclear DNA methylation in relation to mitochondrial heteroplasmy.Nature communications · 2025Article
- The S-depalmitoylase ABHD10 is essential for sperm mitochondrial sheath formation and male fertility.Nature communications · 2025Article
- Recent advances in S-palmitoylation and its emerging roles in human diseases.Journal of hematology & oncology · 2025Review
- Palmitoylation: an emerging therapeutic target bridging physiology and disease.Cellular & molecular biology letters · 2025Review
- The Unconventional Role of ABHD17A in Increasing the S-Palmitoylation and Antiviral Activity of IFITM1 by Downregulating ABHD16A.Biomolecules · 2025Article
- Depalmitoylase ABHD16A negatively regulates the anti-hepatitis B virus activity of IFITM1.Microbiology spectrum · 2025Article
- RNF20/RNF40 supports the aggressive behavior in cervical cancer by regulating a peroxisome-based anti-ferroptotic mechanism.Cell communication and signaling : CCS · 2025Article
- First Steps toward the Design of Peptides that Influence the Intracellular Palmitoylation Machinery.Chembiochem : a European journal of chemical biology · 2025Article
22 more citing papers are in PubMed but not listed here.
Corrections and comments
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Authors and funding
10 authors at 2 institutions in 2 countries.
Funding
Abstract
S-Palmitoylation is a reversible lipid post-translational modification that has been observed on mitochondrial proteins, but both the regulation and functional consequences of mitochondrial S-palmitoylation are poorly understood. Here, we show that perturbing the 'erasers' of S-palmitoylation, acyl protein thioesterases (APTs), with either pan-active inhibitors or a mitochondrial-targeted APT inhibitor, diminishes the antioxidant buffering capacity of mitochondria. Surprisingly, this effect was not mediated by the only known mitochondrial APT, but rather by a resident mitochondrial protein with no known endogenous function, ABHD10. We show that ABHD10 is a member of the APT family of regulatory proteins and identify peroxiredoxin-5 (PRDX5), a key antioxidant protein, as a target of ABHD10 S-depalmitoylase activity. We then find that ABHD10 regulates the S-palmitoylation status of the nucleophilic active site residue of PRDX5, providing a direct mechanistic connection between ABHD10-mediated S-depalmitoylation of PRDX5 and its antioxidant capacity.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.