ArticleNature chemical biology2021
Post-translational insertion of boron in proteins to probe and modulate function.
Article in Nature chemical biology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 18 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
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
18 citing papers in PubMed, 35 citations in OpenAlex.
- Dynamic Anchoring of Peptides to the Extracellular Matrix Enabled by Boronic Acid.Chembiochem : a European journal of chemical biology · 2025Article
- An efficient method for site-selective boronation of peptides and proteins applied in magnified bacterial imaging.Nature communications · 2025Article
- Recent Advancements in the Diversification and Applications of Boron-Containing Compounds in Medicinal Chemistry.Pharmaceuticals (Basel, Switzerland) · 2025Review
- Chemical Carbonylation of Arginine in Peptides and Proteins.Journal of the American Chemical Society · 2025Article
- Ligand-Enabled Selective Coupling of MIDA Boronates to Dehydroalanine-Containing Peptides and Proteins.Journal of the American Chemical Society · 2025Article
- Skin-Integrated Electrogenetic Regulation of Vasculature for Accelerated Wound Healing.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025Article
- Activity of Organoboron Compounds against Biofilm-Forming Pathogens.Antibiotics (Basel, Switzerland) · 2024Review
- Kinetic Resolution of Epimeric Proteins Enables Stereoselective Chemical Mutagenesis.Journal of the American Chemical Society · 2024Article
- Stereospecific Enzymatic Conversion of Boronic Acids to Amines.Journal of the American Chemical Society · 2024Article
- Peptide Boronic Acids by Late-Stage Hydroboration on the Solid Phase.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2024Article
- Cell-Permeable Stimuli-Responsive Ubiquitin Probe for Time-Resolved Monitoring of Substrate Ubiquitination in Live Cells.JACS Au · 2023Article
- Desulfurative Borylation of Small Molecules, Peptides, and Proteins.Journal of the American Chemical Society · 2023Article
- Posttranslational, site-directed photochemical fluorine editing of protein sidechains to probe residue oxidation state viaNature protocols · 2023Review
- Stereoretentive Post-Translational Protein Editing.ACS central science · 2023Article
- Thermal Endurance by a Hot-Spring-Dwelling Phylogenetic Relative of the MesophilicMicrobiology spectrum · 2022Article
- Article
- Umpolung AlaAngewandte Chemie (International ed. in English) · 2022Article
- Reductive site-selective atypicalScience advances · 2022Article
Corrections and comments
- Erratum issued
Authors and funding
11 authors at 3 institutions in 2 countries.
Funding
Abstract
Boron is absent in proteins, yet is a micronutrient. It possesses unique bonding that could expand biological function including modes of Lewis acidity not available to typical elements of life. Here we show that post-translational Cβ-Bγ bond formation provides mild, direct, site-selective access to the minimally sized residue boronoalanine (Bal) in proteins. Precise anchoring of boron within complex biomolecular systems allows dative bond-mediated, site-dependent protein Lewis acid-base-pairing (LABP) by Bal. Dynamic protein-LABP creates tunable inter- and intramolecular ligand-host interactions, while reactive protein-LABP reveals reactively accessible sites through migratory boron-to-oxygen Cβ-Oγ covalent bond formation. These modes of dative bonding can also generate de novo function, such as control of thermo- and proteolytic stability in a target protein, or observation of transient structural features via chemical exchange. These results indicate that controlled insertion of boron facilitates stability modulation, structure determination, de novo binding activities and redox-responsive 'mutation'.
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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.