ArticleACS synthetic biology2018
Genetically Incorporating Two Distinct Post-translational Modifications into One Protein Simultaneously.
Article in ACS synthetic biology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers, 1 of them a synthesis that pooled it.
What it found
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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
34 citing papers in PubMed, 1 synthesis or guideline pooled it, 55 citations in OpenAlex.
- Cell-Free Approach for Non-canonical Amino Acids Incorporation Into Polypeptides.Frontiers in bioengineering and biotechnology · 2020Pooled it
- Noncanonical Amino Acids in Biocatalysis.Chemical reviews · 2024Review
- Deciphering functional roles of protein succinylation and glutarylation using genetic code expansion.Nature chemistry · 2024Article
- Genetic Encoding of Phosphorylated Amino Acids into Proteins.Chemical reviews · 2024Review
- Orthogonal Translation for Site-Specific Installation of Post-translational Modifications.Chemical reviews · 2024Review
- Bacterial protein acetylation: mechanisms, functions, and methods for study.Frontiers in cellular and infection microbiology · 2024Review
- Selective and Site-Specific Incorporation of Nonstandard Amino Acids Within Proteins for Therapeutic Applications.Methods in molecular biology (Clifton, N.J.) · 2024Article
- Dual Noncanonical Amino Acid Incorporation Enabling Chemoselective Protein Modification at Two Distinct Sites in Yeast.Biochemistry · 2023Article
- Studying lysine acetylation of citric acid cycle enzymes by genetic code expansion.Molecular microbiology · 2023Review
- Site-specific dual encoding and labeling of proteins via genetic code expansion.Cell chemical biology · 2023Review
- Functional analysis of protein post-translational modifications using genetic codon expansion.Protein science : a publication of the Protein Society · 2023Review
- Update of the Pyrrolysyl-tRNA Synthetase/tRNAJournal of bacteriology · 2023Review
- "Not-so-popular" orthogonal pairs in genetic code expansion.Protein science : a publication of the Protein Society · 2023Review
- Dual incorporation of non-canonical amino acids enables production of post-translationally modified selenoproteins.Frontiers in molecular biosciences · 2023Article
- High-Throughput Aminoacyl-tRNA Synthetase Engineering for Genetic Code Expansion in Yeast.ACS synthetic biology · 2022Article
- Delivery of the selenoprotein thioredoxin reductase 1 to mammalian cells.Frontiers in molecular biosciences · 2022Article
- A 68-codon genetic code to incorporate four distinct non-canonical amino acids enabled by automated orthogonal mRNA design.Nature chemistry · 2021Article
- Biomolecular simulation based machine learning models accurately predict sites of tolerability to the unnatural amino acid acridonylalanine.Scientific reports · 2021Article
- Introducing noncanonical amino acids for studying and engineering bacterial microcompartments.Current opinion in microbiology · 2021Review
- Genetic Encoding of Three Distinct Noncanonical Amino Acids Using Reprogrammed Initiator and Nonsense Codons.ACS chemical biology · 2021Article
Corrections and comments
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
Abstract
Post-translational modifications (PTMs) play important roles in regulating a variety of biological processes. To facilitate PTM studies, the genetic code expansion strategy has been utilized to cotranslationally incorporate individual PTMs such as acetylation and phosphorylation into proteins at specific sites. However, recent studies have demonstrated that PTMs actually work together to regulate protein functions and structures. Thus, simultaneous incorporation of multiple distinct PTMs into one protein is highly desirable. In this study, we utilized the genetic incorporation systems of phosphoserine and acetyllysine to install both phosphorylation and acetylation into target proteins simultaneously in Escherichia coli. And we used this system to study the effect of coexisting acetylation and phosphorylation on malate dehydrogenase, demonstrating a practical application of this system in biochemical studies. Furthermore, we tested the mutual orthogonality of three widely used genetic incorporation systems, indicating the possibility of incorporating three distinct PTMs into one protein simultaneously.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.