ReviewNature chemistry2016
Expanding the chemical toolbox for the synthesis of large and uniquely modified proteins.
Review in Nature chemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 99 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
99 citing papers in PubMed.
- Site-specific protein functionalization by late-stage reversible cysteine masking.Nature communications · 2026Article
- Phage Display as a Promising Platform for Peptide Drug Discovery.Pharmaceuticals (Basel, Switzerland) · 2026Review
- Advancing protein engineering via organic chemistry.Communications chemistry · 2026Review
- Total Chemical Synthesis of RNF4 by Sequential Native Chemical Ligation: C-To-N Versus N-To-C Strategies.The Journal of organic chemistry · 2026Article
- Engineering Light-Responsive Transcription Factors via Strategic Masking of Post-translational Modification Residues.Bioconjugate chemistry · 2026Article
- Exploring and expanding the chemical multiverse of peptides.Chemical science · 2026Review
- Rapid vinyl thianthrenium tetrafluoroborate-promoted thioacid-based native chemical ligation and its applications in chemical protein synthesis.Communications chemistry · 2026Article
- Chemical Engineering of Transcription Factors Uncovered Cell-Permeable μMax Modulators.Journal of the American Chemical Society · 2025Article
- Examining the Role of Threonine Phosphorylation in Ubiquitin's Function Using Chemical Protein Synthesis.JACS Au · 2025Article
- Review on the o-Aminoaniline Moiety in Peptide and Protein Chemistry.Chembiochem : a European journal of chemical biology · 2025Review
- One-Pot Total Synthesis of a Post-translationally Modified Max Transcription Factor Sheds Light on Ser-Phosphorylation and Lys-Acetylation Crosstalk in DNA Binding.Organic letters · 2025Article
- Unlocking the power of antimicrobial peptides: advances in production, optimization, and therapeutics.Frontiers in cellular and infection microbiology · 2025Review
- Ruthenium-Catalyzed One-pot Peptide Ligation.Methods in molecular biology (Clifton, N.J.) · 2025Article
- Generating a mirror-image monobody targeting MCP-1 via TRAP display and chemical protein synthesis.Nature communications · 2024Article
- An Enabling Peptide Ligation Induced by Thiol-Salicylaldehyde Ester for Chemical Protein Synthesis.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2024Article
- Kinetic and Mechanistic Studies of Native Chemical Ligation with Phenyl α-Selenoester Peptides.JACS Au · 2024Article
- A Versatile Method for Site-Specific Chemical Installation of Aromatic Posttranslational Modification Analogs into Proteins.Journal of the American Chemical Society · 2024Article
- Enhanced native chemical ligation by peptide conjugation in trifluoroacetic acid.Science advances · 2024Article
- Site-Specific Acetylation of the Transcription Factor Protein Max Modulates Its DNA Binding Activity.ACS central science · 2024Article
- Rapid flow-based synthesis of post-translationally modified peptides and proteins: a case study on MYC's transactivation domain.Chemical science · 2024Article
39 more citing papers are in PubMed but not listed here.
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
No grant is acknowledged in the PubMed record.
Abstract
Methods to prepare proteins that include a specific modification at a desired position are essential for understanding their cellular functions and physical properties in living systems. Chemical protein synthesis, which relies on the chemoselective ligation of unprotected peptides, enables the preparation of modified proteins that are not easily fabricated by other methods. In contrast to recombinant approaches, chemical synthesis can be used to prepare protein analogues such as D-proteins, which are useful in protein structure determination and the discovery of novel therapeutics. Post-translationally modifying proteins is another example where chemical protein synthesis proved itself as a powerful approach for preparing samples with high homogeneity and in workable quantities. In this Review, we discuss the basic principles of the field, focusing on novel chemoselective peptide ligation approaches such as native chemical ligation and the recent advances based on this method with a proven record of success in the synthesis of highly important protein targets.
Indexed as
Identifiers
27102674What 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.