ArticleAngewandte Chemie (International ed. in English)2021
Identification of a Bromodomain-like Region in 15-Lipoxygenase-1 Explains Its Nuclear Localization.
Article in Angewandte Chemie (International ed. in English), 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed, 8 citations in OpenAlex.
- Light-Controlled Modulation of 15-Lipoxygenase-1 Regulates Intestinal Inflammatory Signaling.Angewandte Chemie (International ed. in English) · 2026Article
- The Evolution of Fluorescein into A Potential Theranostic Tool.Chemistry (Weinheim an der Bergstrasse, Germany) · 2025Article
- A general approach for activity-based protein profiling of oxidoreductases with redox-differentiated diarylhalonium warheads.Chemical science · 2025Article
- Crafting Molecular Tools for 15-Lipoxygenase-1 in a Single Step.Angewandte Chemie (International ed. in English) · 2025Article
- Acidifiers Attenuate Diquat-Induced Oxidative Stress and Inflammatory Responses by Regulating NF-κB/MAPK/COX-2 Pathways in IPEC-J2 Cells.Antioxidants (Basel, Switzerland) · 2022Article
- Identification of a Bromodomain-like Region in 15-Lipoxygenase-1 Explains Its Nuclear Localization.Angewandte Chemie (International ed. in English) · 2021Article
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Authors and funding
7 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Lipoxygenase (LOX) activity provides oxidative lipid metabolites, which are involved in inflammatory disorders and tumorigenesis. Activity-based probes to detect the activity of LOX enzymes in their cellular context provide opportunities to explore LOX biology and LOX inhibition. Here, we developed Labelox B as a potent covalent LOX inhibitor for one-step activity-based labeling of proteins with LOX activity. Labelox B was used to establish an ELISA-based assay for affinity capture and antibody-based detection of specific LOX isoenzymes. Moreover, Labelox B enabled efficient activity-based labeling of endogenous LOXs in living cells. LOX proved to localize in the nucleus, which was rationalized by identification of a functional bromodomain-like consensus motif in 15-LOX-1. This indicates that 15-LOX-1 is not only involved in oxidative lipid metabolism, but also in chromatin binding, which suggests a potential role in chromatin modifications.
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