ReviewNature reviews. Chemistry2023
Nature-inspired protein ligation and its applications.
Review in Nature reviews. Chemistry, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 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
30 citing papers in PubMed.
- Constrained diffusion-enabled construction of a highly expressed and robust peptide asparaginyl ligase.Chemical science · 2026Article
- A Chemical Framework for Engineering Extracellular Vesicles' Biointerface to Advance Precision Therapeutics.Advanced materials (Deerfield Beach, Fla.) · 2026Review
- Rank-guided learning accelerates automated enzyme engineering.Nature communications · 2026Article
- A programmable living force sensor fabricated with surface engineered microbial network.Nature communications · 2026Article
- Tangled Tail of Mechanically Interlocked Peptides.Journal of the American Chemical Society · 2026Review
- Mining of natural diversity enables efficient and expressible peptide asparaginyl ligases.Nature communications · 2026Article
- Exploiting Selective Position Labeling to Unveil the Hidden Complexity of Terminomics.Molecules (Basel, Switzerland) · 2026Review
- Generating Ultra-Fast Protein trans-Splicing of a Cysteine-Less and Semisynthetic Split Intein for Chemical Protein Labeling.Chembiochem : a European journal of chemical biology · 2026Article
- Methods for studying the effects of phosphorylation patterns in proteins.Biochemical Society transactions · 2026Review
- "Lys-Leu" Motif Empowers ExpedientJACS Au · 2026Article
- Peptide ligase-mediated display: A cell-free platform for tunable selection of affinity peptides.PNAS nexus · 2026Article
- Article
- Protein engineering: status report.Protein engineering, design & selection : PEDS · 2026Review
- Carboxamide: A Privileged Pharmacophore for the Development of Anti-infectious and Anti-cancer Drugs.Current topics in medicinal chemistry · 2026Review
- Article
- Advances in the chemical synthesis of human proteoforms.Science China. Life sciences · 2025Review
- Engineered reactivity of a bacterial E1-like enzyme enables ATP-driven modification of protein and peptide C termini.Nature chemistry · 2025Article
- Introduction of Reactive Thiol Handles into Tyrosine-Tagged Proteins through Enzymatic Oxidative Coupling.Journal of the American Chemical Society · 2025Article
- Differentially labeled flaviviral protease-cofactor complex for NMR spectroscopic applications.Protein expression and purification · 2025Article
- Structural Basis of High-Precision Protein Ligation and Its Application.Journal of the American Chemical Society · 2025Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors.
Funding
Abstract
The ability to manipulate the chemical composition of proteins and peptides has been central to the development of improved polypeptide-based therapeutics and has enabled researchers to address fundamental biological questions that would otherwise be out of reach. Protein ligation, in which two or more polypeptides are covalently linked, is a powerful strategy for generating semisynthetic products and for controlling polypeptide topology. However, specialized tools are required to efficiently forge a peptide bond in a chemoselective manner with fast kinetics and high yield. Fortunately, nature has addressed this challenge by evolving enzymatic mechanisms that can join polypeptides using a diverse set of chemical reactions. Here, we summarize how such nature-inspired protein ligation strategies have been repurposed as chemical biology tools that afford enhanced control over polypeptide composition.
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.