ArticleMethods in molecular biology (Clifton, N.J.)2023
Assaying Arginylation Activity in Cell Lysates Using a Fluorescent Reporter.
Article in Methods in molecular biology (Clifton, N.J.), 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.
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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.
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Who cites it
2 citing papers in PubMed, 0 citations in OpenAlex.
- Divergent contributions of multiple PPIases to cell survival, sociality, and stress tolerance inApplied and environmental microbiology · 2026Article
- The C-terminal domain of yeast Arginyltransferase1 is essential for its catalytic activity.FEBS open bio · 2026Article
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Authors and funding
2 authors at 2 institutions in 2 countries.
Funding
Abstract
Here, we describe an antibody-based method to evaluate the enzymatic activity of arginyltransferase1 (Ate1). The assay is based on the arginylation of a reporter protein, which contains the N-terminal peptide of beta-actin, a known endogenous substrate of Ate1, and a C-terminal GFP. The arginylation level of the reporter protein is determined on an immunoblot with an antibody specific for the arginylated N-terminus, while the total amount of substrate is evaluated with anti-GFP antibody. This method can be used to conveniently and accurately examine the Ate1 activity in yeast and mammalian cell lysates. Moreover, the effect of mutation on Ate1 critical residues and effect of stress and other factors on Ate1 activity can also be successfully determined with this method.
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