ArticleAngewandte Chemie (International ed. in English)2022
Cysteine-Assisted Click-Chemistry for Proximity-Driven, Site-Specific Acetylation of Histones.
Article in Angewandte Chemie (International ed. in English), 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 14 citations in OpenAlex.
- Toward Ideal Proximity-Driven Reactions in Chemical Biology.Chembiochem : a European journal of chemical biology · 2026Review
- Toward Precision Bioconjugation: Chemical Strategies for Site-Selective Cysteine Conjugation.Precision chemistry · 2026Review
- Recent advances in site-specific modifications of peptides and proteins.Chemical science · 2026Review
- Advances in Proximity-Assisted Bioconjugation.Accounts of chemical research · 2025Review
- NSPs: chromogenic linkers for fast, selective, and irreversible cysteine modification.Chemical science · 2024Article
- Inserting "OFF-to-ON" BODIPY Tags into Cytokines: A Fluorogenic Interleukin IL-33 for Real-Time Imaging of Immune Cells.ACS central science · 2024Article
- Epigenetics of hypertension as a risk factor for the development of coronary artery disease in type 2 diabetes mellitus.Frontiers in endocrinology · 2024Review
- Cysteine-Assisted Click-Chemistry for Proximity-Driven, Site-Specific Acetylation of Histones.Angewandte Chemie (International ed. in English) · 2022Article
Corrections and comments
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Authors and funding
7 authors at 1 institution in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Post-translational modifications of histones are essential in the regulation of chromatin structure and function. Among these modifications, lysine acetylation is one of the most established. Earlier studies relied on the use of chromatin containing heterogeneous mixtures of histones acetylated at multiple sites. Differentiating the individual contribution of single acetylation events towards chromatin regulation is thus of great relevance. However, it is difficult to access homogeneous samples of histones, with a single acetylation, in sufficient quantities for such studies. By engineering histone H3 with a cysteine in proximity of the lysine of interest, we demonstrate that conjugation with maleimide-DBCO followed by a strain-promoted alkyne-azide cycloaddition reaction results in the acetylation of a single lysine in a controlled, site-specific manner. The chemical precision offered by our click-to-acetylate approach will facilitate access to and the study of acetylated histones.
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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.