ArticleFrontiers in plant science2022
A Continuous Assay Set to Screen and Characterize Novel Protein N-Acetyltransferases Unveils Rice General Control Non-repressible 5-Related N-Acetyltransferase2 Activity.
Article in Frontiers in plant science, 2022. 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, 11 citations in OpenAlex.
- Rubisco functional integrity requires a dedicated three-step maturation pathway.Science advances · 2026Article
- Glucoselipid Biosurfactant Biosynthesis Operon ofMicroorganisms · 2025Article
- Purification and activity assays of N-terminal acetyltransferase D.Methods in enzymology · 2025Article
- The Global Acetylation Profiling Pipeline for Quick Assessment of Protein N-Acetyltransferase Specificity In Cellulo.Methods in molecular biology (Clifton, N.J.) · 2023Article
- Tracking N-terminal protein processing from the Golgi to the chromatophore of a rhizarian amoeba.Plant physiology · 2022Article
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Authors and funding
6 authors at 4 institutions in 1 country.
Funding
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Abstract
Protein N-acetyltransferases (NATs) belong to the general control non-repressible 5 (Gcn5)-related N-acetyltransferases (GNATs) superfamily. GNATs catalyze the transfer of acetyl from acetyl-CoA to the reactive amine moiety of a wide range of acceptors. NAT sequences are difficult to distinguish from other members of the GNAT superfamily and there are many uncharacterized GNATs. To facilitate the discovery and characterization of new GNATs, we have developed a new continuous, non-radioactive assay. This assay is virtually independent of the substrate and can be used to get substrate specificity hints. We validated first the assay with the well-characterized
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