ArticleACS chemical biology2018
HDAC1 Substrate Profiling Using Proteomics-Based Substrate Trapping.
Article in ACS chemical biology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
What it found
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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.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
17 citing papers in PubMed, 26 citations in OpenAlex.
- Replication associated nuclear DNA mismatch repair across kingdoms.Biochemical Society transactions · 2026Review
- HDAC11 Deacetylates BRAF to Regulate Kinase Activity and Cell Proliferation.ACS chemical biology · 2025Article
- Metformin sensitizes triple-negative breast cancer to histone deacetylase inhibitors by targeting FGFR4.Journal of biomedical science · 2025Article
- Novel Sulforaphane Analog Disrupts Phosphatidylinositol-3-Kinase-Protein Kinase B Pathway and Inhibits Cancer Cell Progression via Reactive Oxygen Species-Mediated Caspase-Independent Apoptosis.ACS pharmacology & translational science · 2024Article
- Interactions of Histone Deacetylase 6 with DNA Damage Repair Factors Strengthen its Utility as a Combination Drug Target in High-Grade Serous Ovarian Cancer.ACS pharmacology & translational science · 2023Article
- GSE1 links the HDAC1/CoREST co-repressor complex to DNA damage.Nucleic acids research · 2023Article
- Activity Guided Azide-methyllysine Photo-trapping for Substrate Profiling of Lysine Demethylases.Journal of the American Chemical Society · 2023Article
- Proteomics-based trapping with single or multiple inactive mutants reproducibly profiles histone deacetylase 1 substrates.Journal of proteomics · 2023Article
- Tau-dependent HDAC1 nuclear reduction is associated with altered VGluT1 expression.Frontiers in cell and developmental biology · 2023Article
- A comprehensive mouse brain acetylome-the cellular-specific distribution of acetylated brain proteins.Frontiers in cellular neuroscience · 2022Article
- HDAC6 Substrate Discovery Using Proteomics-Based Substrate Trapping: HDAC6 Deacetylates PRMT5 to Influence Methyltransferase Activity.ACS chemical biology · 2021Article
- Differential profiles of HDAC1 substrates and associated proteins in breast cancer cells revealed by trapping.Molecular omics · 2021Article
- Review
- Targeting epigenetic regulators in the treatment of T-cell lymphoma.Expert review of hematology · 2020Review
- Acetylation and Deacetylation of DNA Repair Proteins in Cancers.Frontiers in oncology · 2020Review
- Hypoxia-Inducible Lysine Methyltransferases: G9a and GLP Hypoxic Regulation, Non-histone Substrate Modification, and Pathological Relevance.Frontiers in genetics · 2020Review
- Optimal Substrate-Trapping Mutants to Discover Substrates of HDAC1.Chembiochem : a European journal of chemical biology · 2019Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Histone deacetylase (HDAC) proteins are overexpressed in multiple diseases, including cancer, and have emerged as anticancer drug targets. HDAC proteins regulate cellular processes, such as the cell cycle, apoptosis, and cell proliferation, by deacetylating histone and non-histone substrates. Although a plethora of acetylated proteins have been identified using large-scale proteomic approaches, the HDAC proteins responsible for their dynamic deacetylation have been poorly studied. For example, few substrates of HDAC1 have been identified, which is mainly due to the scarcity of substrate identification tools. We recently developed a mutant trapping strategy to identify novel substrates of HDAC1. Herein, we introduce an improved version of the trapping method that uses mass spectrometry (MS)-based proteomics to identify multiple substrates simultaneously. Among the substrate hits, CDK1, AIFM1, MSH6, and RuvB-like 1 were identified as likely HDAC1 substrates. These newly discovered HDAC1 substrates are involved in various biological processes, suggesting novel functions of HDAC1 apart from epigenetics. Substrate trapping combined with MS-based proteomics provides an efficient approach to HDAC1 substrate identification and contributes to the full characterization of HDAC function in normal and disease states.
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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.