ReviewMolecules (Basel, Switzerland)2018
Recent Development of Genetic Code Expansion for Posttranslational Modification Studies.
Review in Molecules (Basel, Switzerland), 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
23 citing papers in PubMed.
- Genetic Code Expansion Approaches to Decipher the Ubiquitin Code.Chemical reviews · 2024Review
- Review
- Orthogonal Translation for Site-Specific Installation of Post-translational Modifications.Chemical reviews · 2024Review
- Posttranslational, site-directed photochemical fluorine editing of protein sidechains to probe residue oxidation state viaNature protocols · 2023Review
- Functional analysis of protein post-translational modifications using genetic codon expansion.Protein science : a publication of the Protein Society · 2023Review
- "Not-so-popular" orthogonal pairs in genetic code expansion.Protein science : a publication of the Protein Society · 2023Review
- Engineering enzyme activity using an expanded amino acid alphabet.Protein engineering, design & selection : PEDS · 2023Article
- Modulation of plant acetyl-CoA synthetase activity by post-translational lysine acetylation.Frontiers in molecular biosciences · 2023Article
- Dual incorporation of non-canonical amino acids enables production of post-translationally modified selenoproteins.Frontiers in molecular biosciences · 2023Article
- A peptide-crosslinking approach identifies HSPA8 and PFKL as selective interactors of an actin-derived peptide containing reduced and oxidized methionine.RSC chemical biology · 2022Article
- Substitution of the sole tryptophan of the cupredoxin, amicyanin, with 5-hydroxytryptophan alters fluorescence properties and energy transfer to the type 1 copper site.Journal of inorganic biochemistry · 2022Article
- Tuning the Properties of Protein-Based Polymers Using High-Performance Orthogonal Translation Systems for the Incorporation of Aromatic Non-Canonical Amino Acids.Frontiers in bioengineering and biotechnology · 2022Article
- Lactylation, an emerging hallmark of metabolic reprogramming: Current progress and open challenges.Frontiers in cell and developmental biology · 2022Review
- Writing and erasing O-GlcNAc from target proteins in cells.Biochemical Society transactions · 2021Article
- Pyrimidine Biosynthetic Enzyme CAD: Its Function, Regulation, and Diagnostic Potential.International journal of molecular sciences · 2021Review
- Biomolecular simulation based machine learning models accurately predict sites of tolerability to the unnatural amino acid acridonylalanine.Scientific reports · 2021Article
- Chemogenetic and optogenetic control of post-translational modifications through genetic code expansion.Current opinion in chemical biology · 2021Review
- Proposal of the Annotation of Phosphorylated Amino Acids and Peptides Using Biological and Chemical Codes.Molecules (Basel, Switzerland) · 2021Article
- Acetylation at Lysine 86 ofFrontiers in microbiology · 2021Article
- Enhancing the incorporation of lysine derivatives into proteins with methylester forms of unnatural amino acids.Bioorganic & medicinal chemistry letters · 2020Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Nowadays advanced mass spectrometry techniques make the identification of protein posttranslational modifications (PTMs) much easier than ever before. A series of proteomic studies have demonstrated that large numbers of proteins in cells are modified by phosphorylation, acetylation and many other types of PTMs. However, only limited studies have been performed to validate or characterize those identified modification targets, mostly because PTMs are very dynamic, undergoing large changes in different growth stages or conditions. To overcome this issue, the genetic code expansion strategy has been introduced into PTM studies to genetically incorporate modified amino acids directly into desired positions of target proteins. Without using modifying enzymes, the genetic code expansion strategy could generate homogeneously modified proteins, thus providing powerful tools for PTM studies. In this review, we summarized recent development of genetic code expansion in PTM studies for research groups in this field.
Indexed as
Identifiers
What OpenQuestion holds
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.