ArticleJournal of the American Chemical Society2009
Selective recognition of protein tetraserine motifs with a cell-permeable, pro-fluorescent bis-boronic acid.
Article in Journal of the American Chemical Society, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 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.
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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.
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Who cites it
44 citing papers in PubMed, 177 citations in OpenAlex.
- Site-Specific Protein Bioconjugation Through Cellular Incorporation of Noncanonical Amino Acids.Angewandte Chemie (International ed. in English) · 2026Review
- Light-Based Molecular Tools to Precisely Monitor and Operate β-Adrenoceptors.Medicinal research reviews · 2026Review
- Peptide Tags for Site-Selective Nonenzymatic Covalent Modification of Proteins.Journal of peptide science : an official publication of the European Peptide Society · 2025Review
- Advancing Single-Molecule Biophysics: Next-Generation Organic Fluorophores with Tailored Labeling Strategies.Chemical & biomedical imaging · 2025Review
- Live imaging of the extracellular matrix with a glycan-binding fluorophore.Nature methods · 2025Article
- Noncanonical Amino Acid Tools and Their Application to Membrane Protein Studies.Chemical reviews · 2024Review
- Imaging the extracellular matrix in live tissues and organisms with a glycan-binding fluorophore.bioRxiv : the preprint server for biology · 2024Article
- Visualizing the invisible: novel approaches to visualizing bacterial proteins and host-pathogen interactions.Frontiers in bioengineering and biotechnology · 2024Review
- Reductive site-selective atypicalScience advances · 2022Article
- An overview of chemo- and site-selectivity aspects in the chemical conjugation of proteins.Royal Society open science · 2022Article
- Strategies for Site-Specific Labeling of Receptor Proteins on the Surfaces of Living Cells by Using Genetically Encoded Peptide Tags.Chembiochem : a European journal of chemical biology · 2021Review
- Broad Applications of Thiazole Orange in Fluorescent Sensing of Biomolecules and Ions.Molecules (Basel, Switzerland) · 2021Review
- MiniVIPER Is a Peptide Tag for Imaging and Translocating Proteins in Cells.Biochemistry · 2020Article
- Selective N-terminal acylation of peptides and proteins with a Gly-His tag sequence.Nature communications · 2018Article
- Site-Selective Cysteine-Cyclooctyne Conjugation.Angewandte Chemie (International ed. in English) · 2018Article
- Article
- A structural and mechanistic study of π-clamp-mediated cysteine perfluoroarylation.Scientific reports · 2017Article
- Boronic acids as tools to study (plant) developmental processes?Plant signaling & behavior · 2017Article
- A Critical and Comparative Review of Fluorescent Tools for Live-Cell Imaging.Annual review of physiology · 2017Review
- Site-Specific Bioorthogonal Labeling for Fluorescence Imaging of Intracellular Proteins in Living Cells.Journal of the American Chemical Society · 2016Article
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
There is considerable interest in novel cell imaging tools that avoid the use of fluorescent proteins. One widely used class of such reagents are "pro-fluorescent" biarsenical dyes such as FlAsH, ReAsH, CrAsH, and Cy3As. Despite their utility, biarsenicals are plagued by high background labeling and cytotoxicity and are challenging to apply in oxidizing cellular locale. Here we demonstrate that [(3-oxospiro[isobenzofuran-1(3H),9'-[9H]xanthene]-3',6'-diyl)bis(iminomethylene-2,1-phenylene)]bis-(9CI), a rhodamine-derived bisboronic acid (RhoBo) described initially as a monosaccharide sensor, functions as a cell-permeable, turn-on fluorescent sensor for tetraserine motifs in recombinant proteins. RhoBo binds peptides or proteins containing Ser-Ser-Pro-Gly-Ser-Ser with affinities in the nanomolar concentration range and prefers this sequence to simple monosaccharides by >10,000-fold. RhoBo fails to form fluorescent complexes with constituents of the mammalian cell surface, as judged by epifluorescent, confocal, and TIRF microscopy, but fluoresces brightly within the Ser-Ser-Pro-Gly-Ser-Ser-rich cell interior. These results suggest that current efforts to identify optimal serine-rich sequences for RhoBo will allow it to function effectively as a selective small-molecule label for appropriately tagged proteins either upon or within living cells.
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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.