ReviewJournal of peptide science : an official publication of the European Peptide Society2025
Peptide Tags for Site-Selective Nonenzymatic Covalent Modification of Proteins.
Review in Journal of peptide science : an official publication of the European Peptide Society, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 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
2 citing papers in PubMed.
- Thiol-Retaining N-Terminal Cysteine Chemistry for Dual Modification and Bicyclic Peptide Construction.Journal of the American Chemical Society · 2026Article
- Peptide Tags for Site-Selective Nonenzymatic Covalent Modification of Proteins.Journal of peptide science : an official publication of the European Peptide Society · 2025Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors.
Funding
Abstract
Bioconjugation chemistry is an important tool for studying proteins, developing pharmaceutical agents, and for many other applications. Conventional methods for protein functionalization rely on chemoselective reactions but often have poor regioselectivity. Peptide tags facilitating site-selective chemical covalent modification of proteins are of great value in the synthesis of protein conjugates. Ideally, a protein would only have to be minimally mutated prior to chemical modification to avoid interfering with native protein folding, trafficking, and function. This short review summarizes the advances in the developments and applications of peptide tags for covalent modifications that proceed without enzymatic assistance.
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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.