ReviewExperimental & molecular medicine2018
Versatility of ARD1/NAA10-mediated protein lysine acetylation.
Review in Experimental & molecular medicine, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
What it found
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Who cites it
14 citing papers in PubMed, 16 citations in OpenAlex.
- NAA10 and BTRC drive CREBRF degradation in endoplasmic reticulum stress and renal tubular injury.Journal of diabetes investigation · 2026Article
- UBE2M promotes malignant phenotypes of prostate cancer through mediating NAA10 neddylation.Journal of translational medicine · 2026Article
- Proteogenomic Characterization Reveals Subtype-Specific Therapeutic Potential for HER2-Low Breast Cancer.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Article
- Decoding Epigenetic Switches: How Histone Acetylation/Deacetylation Regulates Mononuclear/Macrophage Fate in Bone Disorders.International journal of biological sciences · 2026Review
- NAA10 (N-Alpha-Acetyltransferase 10): A Multifunctional Regulator in Development, Disease, and Cancer.Cells · 2025Review
- NAA10 (N-Alpha-Acetyltransferase 10): A Multifunctional Regulator in Development, Disease, and Cancer.Cells · 2025Review
- Molecular Mechanisms of ARD1 in Tumors.Cancer medicine · 2025Review
- Potential Utility ofGenes · 2024Article
- Dysregulation of lysine acetylation in the pathogenesis of digestive tract cancers and its clinical applications.Frontiers in cell and developmental biology · 2024Review
- Article
- Lysine Acetyltransferases and Their Role in AR Signaling and Prostate Cancer.Frontiers in endocrinology · 2022Review
- NAA10 as a New Prognostic Marker for Cancer Progression.International journal of molecular sciences · 2020Review
- Characterization of Lysine Acetyltransferase Activity of Recombinant Human ARD1/NAA10.Molecules (Basel, Switzerland) · 2020Article
- Spotlight on protein N-terminal acetylation.Experimental & molecular medicine · 2018Review
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Post-translational modifications (PTMs) are chemical alterations that occur in proteins that play critical roles in various cellular functions. Lysine acetylation is an important PTM in eukaryotes, and it is catalyzed by lysine acetyltransferases (KATs). KATs transfer acetyl-coenzyme A to the internal lysine residue of substrate proteins. Arrest defective 1 (ARD1) is a member of the KAT family. Since the identification of its KAT activity 15 years ago, many studies have revealed that diverse cellular proteins are acetylated by ARD1. ARD1-mediated lysine acetylation is a key switch that regulates the enzymatic activities and biological functions of proteins and influences cell biology from development to pathology. In this review, we summarize protein lysine acetylation mediated by ARD1 and describe the biological meanings of this modification.
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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.