ArticleScientific reports2018
LC-MS/MS-based quantitative study of the acyl group- and site-selectivity of human sirtuins to acylated nucleosomes.
Article in Scientific reports, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 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
28 citing papers in PubMed, 53 citations in OpenAlex.
- Precision Chemistry for Protein Lysine Modification.Chemistry (Weinheim an der Bergstrasse, Germany) · 2026Review
- Novel protein acylations in Alzheimer's disease: Molecular, mechanisms, biological significance, and diagnostic and therapeutic potentials.Journal of advanced research · 2026Review
- Beyond deacetylation: crosstalk mechanisms and context-dependent regulation of sirtuin non-classical enzymatic functions in disease.Molecular medicine (Cambridge, Mass.) · 2026Review
- Current Understanding of SIRT7 Function and Its Emerging Roles in the Central Nervous System.Cells · 2026Review
- Structural basis of SIRT2 pre-catalysis NADRSC chemical biology · 2025Article
- A Method for Constructing Nucleosome Arrays with Spatially Defined Histone PTMs and DNA Damage.Angewandte Chemie (International ed. in English) · 2025Article
- SIRT7 Is a Lysine Deacylase with a Preference for Depropionylation and Demyristoylation.International journal of molecular sciences · 2025Article
- Structural basis of SIRT7 nucleosome engagement and substrate specificity.Nature communications · 2025Article
- Cracking Lysine Crotonylation (Kcr): Enlightening a Promising Post-Translational Modification.Chembiochem : a European journal of chemical biology · 2025Review
- Article
- The dark side of SIRT7.Molecular and cellular biochemistry · 2024Review
- YZL-51N functions as a selective inhibitor of SIRT7 by NADiScience · 2024Article
- Review
- A glimpse into novel acylations and their emerging role in regulating cancer metastasis.Cellular and molecular life sciences : CMLS · 2024Review
- SIRT7: the seventh key to unlocking the mystery of aging.Physiological reviews · 2024Review
- Functions and mechanisms of protein lysine butyrylation (Kbu): Therapeutic implications in human diseases.Genes & diseases · 2023Review
- Investigating Physiopathological Roles for Sirtuins in a Mouse Model.Methods in molecular biology (Clifton, N.J.) · 2023Article
- Evaluation of acyllysine isostere interactions with the aromatic pocket of the AF9 YEATS domain.Protein science : a publication of the Protein Society · 2023Article
- Cysteine-Assisted Click-Chemistry for Proximity-Driven, Site-Specific Acetylation of Histones.Angewandte Chemie (International ed. in English) · 2022Article
- Insulin-like growth factor binding proteins 7 prevents dental pulp-derived mesenchymal stem cell senescence via metabolic downregulation of p21.Science China. Life sciences · 2022Article
Corrections and comments
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Authors and funding
7 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Chromatin structure and gene expression are dynamically regulated by posttranslational modifications of histones. Recent advance in mass spectrometry has identified novel types of lysine acylations, such as butyrylation and malonylation, whose functions and regulations are likely different from those of acetylation. Sirtuins, nicotinamide adenine dinucleotide (NAD
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What OpenQuestion holds
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.