ReviewAngewandte Chemie (International ed. in English)2016
From Chemical Mutagenesis to Post-Expression Mutagenesis: A 50 Year Odyssey.
Review in Angewandte Chemie (International ed. in English), 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 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
21 citing papers in PubMed.
- Site-specific protein functionalization by late-stage reversible cysteine masking.Nature communications · 2026Article
- Desulfurative modification of cysteine residues in peptides and proteinsChemical science · 2025Article
- A Versatile Method for Site-Specific Chemical Installation of Aromatic Posttranslational Modification Analogs into Proteins.Journal of the American Chemical Society · 2024Article
- Carbon-Centered Radicals in Protein Manipulation.ACS central science · 2023Review
- Modular Diazo Compound for the Bioreversible Late-Stage Modification of Proteins.Journal of the American Chemical Society · 2023Article
- Stereoretentive Post-Translational Protein Editing.ACS central science · 2023Article
- Posttranslational Chemical Mutagenesis Methods to Insert Posttranslational Modifications into Recombinant Proteins.Molecules (Basel, Switzerland) · 2022Review
- Systematic Activity Maturation of a Single-Domain Antibody with Non-canonical Amino Acids through Chemical Mutagenesis.Cell chemical biology · 2021Article
- Site-specific chemical fatty-acylation for gain-of-function analysis of protein S-palmitoylation in live cells.Chemical communications (Cambridge, England) · 2020Article
- Article
- Site-Selective and Rewritable Labeling of DNA through Enzymatic, Reversible, and Click Chemistries.ACS central science · 2020Article
- Concepts of Catalysis in Site-Selective Protein Modifications.Journal of the American Chemical Society · 2019Review
- Chemoenzymatic Methods for the Synthesis of Glycoproteins.Chemical reviews · 2018Review
- Article
- Total chemical synthesis, refolding, and crystallographic structure of fully active immunophilin calstabin 2 (FKBP12.6).Protein science : a publication of the Protein Society · 2016Article
- Piperidine-based glycodendrons as protein N-glycan prosthetics.Bioorganic & medicinal chemistry · 2016Article
- Chloromethyl-triazole: a new motif for site-selective pseudo-acylation of proteins.Chemical communications (Cambridge, England) · 2016Article
- Xenomicrobiology: a roadmap for genetic code engineering.Microbial biotechnology · 2016Review
- From Chemical Mutagenesis to Post-Expression Mutagenesis: A 50 Year Odyssey.Angewandte Chemie (International ed. in English) · 2016Review
- Deciphering the dynamic code: DNA recognition by transcription factors in the ever-changing genome.TranscriptionReview
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
Site-directed (gene) mutagenesis has been the most useful method available for the conversion of one amino acid residue of a given protein into another. Until relatively recently, this strategy was limited to the twenty standard amino acids. The ongoing maturation of stop codon suppression and related technologies for unnatural amino acid incorporation has greatly expanded access to nonstandard amino acids by expanding the scope of the translational apparatus. However, the necessity for translation of genetic changes restricts the diversity of residues that may be incorporated. Herein we highlight an alternative approach, termed post-expression mutagenesis, which operates at the level of the very functional biomolecules themselves. Using the lens of retrosynthesis, we highlight prospects for new strategies in protein modification, alteration, and construction which will enable protein science to move beyond the constraints of the "translational filter" and lead to a true synthetic biology.
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.