ArticleNature chemical biology2015
One-step site-specific modification of native proteins with 2-pyridinecarboxyaldehydes.
Article in Nature chemical biology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 107 papers.
What it found
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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
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Who cites it
107 citing papers in PubMed.
- N-Terminal protein sequencing by nicotinic acid derivatization and MS analysis.Analytical and bioanalytical chemistry · 2026Article
- 4-Formyl-N-Methylpyridinium-Mediated N-Terminal Cysteine Modification/Removal Facilitates One-Pot Multiplex Peptide Ligation.Angewandte Chemie (International ed. in English) · 2026Article
- An acid-responsive rhodamine-based fluorescent probe for N-terminal protein labeling and aqueous Tsuji-Trost allylic alkylation.Molecular diversity · 2026Article
- Pyrene-Conjugated, 2-Pyridinecarboxaldehyde Derivatives as N-Terminus-Specific Tags for MALDI- and LALDI-MS.Rapid communications in mass spectrometry : RCM · 2026Article
- Protein-Protein Cross-Linking by a DNA Damage-Derived Histone Modification.Journal of the American Chemical Society · 2026Article
- Exploiting Selective Position Labeling to Unveil the Hidden Complexity of Terminomics.Molecules (Basel, Switzerland) · 2026Review
- Creating unimolecular multivalent diversity in protein conjugates via the Passerini multicomponent bioconjugation with isocyanoproteins.Communications chemistry · 2026Article
- Enzyme Immobilization in Porous Crystals via Cage Encapsulation.Angewandte Chemie (International ed. in English) · 2025Article
- Unraveling the Conformational and Electronic Landscape of 3‑Pyridinecarboxaldehyde: A Spectroscopic Journey through Conformer-Specific Ionization.ACS physical chemistry Au · 2025Article
- Efficient Synthesis of Chemically Recyclable Polyamides via Substituent Effects-Enabled Mechanistic Pathway.Angewandte Chemie (International ed. in English) · 2025Article
- Peptide Tags for Site-Selective Nonenzymatic Covalent Modification of Proteins.Journal of peptide science : an official publication of the European Peptide Society · 2025Review
- Profiling the proteome-wide selectivity of diverse electrophiles.Nature chemistry · 2025Article
- Catalysis in Chemical Modification of Proteins.ChemCatChem · 2025Article
- The chemical language of protein glycation.Nature chemical biology · 2025Review
- Decoding aptamer-protein binding kinetics for continuous biosensing using single-molecule techniques.Science advances · 2025Article
- One-Step Maleimide-Based Dual Functionalization of Protein N-Termini.Angewandte Chemie (International ed. in English) · 2025Article
- Late-Stage Reshaping of Phage-Displayed Libraries to Macrocyclic and Bicyclic Landscapes using a Multipurpose Linchpin.Journal of the American Chemical Society · 2025Article
- Target Bioconjugation of Protein Through Chemical, Molecular Dynamics, and Artificial Intelligence Approaches.Metabolites · 2024Review
- Resolving Sulfation Posttranslational Modifications on a Peptide Hormone using Nanopores.ACS nano · 2024Article
- O-GlcNAc modification of HSP27 alters its protein interactions and promotes refolding of proteins through the BAG3/HSP70 co-chaperone.Protein science : a publication of the Protein Society · 2024Article
47 more citing papers are in PubMed but not listed here.
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Authors and funding
4 authors.
Funding
Abstract
The chemical modification of proteins is an enabling technology for many scientific fields, including chemical biology, biophysics, bioengineering and materials science. These methods allow the attachment of strategically selected detection probes, polymers, drug molecules and analysis platforms. However, organic reactions that can proceed under conditions mild enough to maintain biomolecular function are limited. Even more rare are chemical strategies that can target a single site, leading to products with uniform properties and optimal function. We present a versatile method for the selective modification of protein N termini that does not require any genetic engineering of the protein target. This reaction is demonstrated for 12 different proteins, including the soluble domain of the human estrogen receptor. The function of this protein was confirmed through the binding of a fluorescent estrogen mimic, and the modified protein was explored as a prototype for the detection of endocrine-disrupting chemicals in water.
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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.