ArticleAngewandte Chemie (International ed. in English)2024
A Site-Specific Click Chemistry Approach to Di-Ubiquitylate H1 Variants Reveals Position-Dependent Stimulation of the DNA Repair Protein RNF168.
Article in Angewandte Chemie (International ed. in English), 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed.
- Advancements and applications of click chemistry in protein labeling and bioconjugation.RSC advances · 2026Review
- Synthesis and antitumor property of triazole-aryloxyacetyl hydrazide hybrids with furo[2,3-d]pyrimidine scaffold.BMC chemistry · 2026Article
- Structural insights into γH2Ax containing nucleosomes.Nucleic acids research · 2025Article
- Review
- A Site-Specific Click Chemistry Approach to Di-Ubiquitylate H1 Variants Reveals Position-Dependent Stimulation of the DNA Repair Protein RNF168.Angewandte Chemie (International ed. in English) · 2024Article
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3 authors.
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Abstract
Ubiquitylation of histone H2A at lysines 13 and 15 by the E3 ligase RNF168 plays a key role in orchestrating DNA double-strand break (DSB) repair, which is often deregulated in cancer. RNF168 activity is triggered by DSB signaling cascades, reportedly through K63-linked poly-ubiquitylation of linker histone H1. However, direct experimental evidence of this mechanism has been elusive, primarily due to the lack of methods to specifically poly-ubiquitylate H1. Here, we developed a versatile click chemistry approach to covalently link multiple proteins in a site-specific, controlled, and stepwise manner. Applying this method, we synthesized H1 constructs bearing triazole-linked di-ubiquitin on four DNA repair-associated ubiquitylation hotspots (H1
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