ArticleProtein science : a publication of the Protein Society2019
The cysteine-free single mutant C32S of APEX2 is a highly expressed and active fusion tag for proximity labeling applications.
Article in Protein science : a publication of the Protein Society, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 12 citations in OpenAlex.
- Directed Evolution Improves the Catalytic Efficiency of APEX2-Mediated Proximity-Dependent RNA Labeling.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Article
- Hat1 Orchestrates Heterochromatin Inheritance by Regulating Localization of H3K9 Methyltransferases.bioRxiv : the preprint server for biology · 2026Article
- Review
- Proximity Labeling in Plants.Annual review of plant biology · 2023Review
- Proximity Protein Labeling InJournal of biological methods · 2023Article
- Advances in enzyme-mediated proximity labeling and its potential for plant research.Plant physiology · 2022Article
- Proximity labeling for investigating protein-protein interactions.Methods in cell biology · 2022Article
- Recent progress in mass spectrometry-based strategies for elucidating protein-protein interactions.Cellular and molecular life sciences : CMLS · 2021Review
- Proximity-dependent labeling methods for proteomic profiling in living cells: An update.Wiley interdisciplinary reviews. Developmental biology · 2021Review
- The cysteine-free single mutant C32S of APEX2 is a highly expressed and active fusion tag for proximity labeling applications.Protein science : a publication of the Protein Society · 2019Article
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Authors and funding
6 authors at 2 institutions in 1 country.
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Abstract
APEX2, an engineered ascorbate peroxidase for high activity, is a powerful tool for proximity labeling applications. Owing to its lack of disulfides and the calcium-independent activity, APEX2 can be applied intracellularly for targeted electron microscopy imaging or interactome mapping when fusing to a protein of interest. However, APEX2 fusion is often deleterious to the protein expression, which seriously hampers its wide utility. This problem is especially compelling when APEX2 is fused to structurally delicate proteins, such as multi-pass membrane proteins. In this study, we found that a cysteine-free single mutant C32S of APEX2 dramatically improved the expression of fusion proteins in mammalian cells without compromising the enzyme activity. We fused APEX2 and APEX2
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