ArticleNature biotechnology2004
Reversible site-selective labeling of membrane proteins in live cells.
Article in Nature biotechnology, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 64 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.
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Who cites it
64 citing papers in PubMed.
- A high-affinity split-HaloTag for live-cell protein labeling.Nature communications · 2026Article
- Peptide Tags for Site-Selective Nonenzymatic Covalent Modification of Proteins.Journal of peptide science : an official publication of the European Peptide Society · 2025Review
- Review
- Review
- Maturation strategy influences expression levels and cofactor occupancy in Fe-S proteins.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2023Article
- Design and Synthesis of Porphyrin-Nitrilotriacetic Acid Dyads with Potential Applications in Peptide Labeling through Metallochelate Coupling.ACS omega · 2022Article
- A comprehensive comparison between camelid nanobodies and single chain variable fragments.Biomarker research · 2021Review
- 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
- Simplified detection of polyhistidine-tagged proteins in gels and membranes using a UV-excitable dye and a multiple chelator head pair.The Journal of biological chemistry · 2020Article
- Single-Virus Tracking: From Imaging Methodologies to Virological Applications.Chemical reviews · 2020Review
- Recognition of Proteins by Metal Chelation-Based Fluorescent Probes in Cells.Frontiers in chemistry · 2019Review
- Chemogenetic Approach Using Ni(II) Complex-Agonist Conjugates Allows Selective Activation of Class A G-Protein-Coupled Receptors.ACS central science · 2018Article
- New Routes and Opportunities for Modular Construction of Particulate Vaccines: Stick, Click, and Glue.Frontiers in immunology · 2018Review
- Label-Free Direct Electrical Detection of a Histidine-Rich Protein with Sub-Femtomolar Sensitivity using an Organic Field-Effect Transistor.ChemistryOpen · 2017Article
- Chemical labelling for visualizing native AMPA receptors in live neurons.Nature communications · 2017Article
- Nanobody Technology: A Versatile Toolkit for Microscopic Imaging, Protein-Protein Interaction Analysis, and Protein Function Exploration.Frontiers in immunology · 2017Review
- Subcellular functions of proteins under fluorescence single-cell microscopy.Biochimica et biophysica acta · 2016Review
- Modulation of Intracellular Quantum Dot to Fluorescent Protein Förster Resonance Energy Transfer via Customized Ligands and Spatial Control of Donor-Acceptor Assembly.Sensors (Basel, Switzerland) · 2015Article
- Diffusion coefficients and dissociation constants of enhanced green fluorescent protein binding to free standing membranes.Data in brief · 2015Article
- Protein recognition by bivalent, 'turn-on' fluorescent molecular probes.Chemical science · 2015Article
4 more citing papers are in PubMed but not listed here.
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Authors and funding
3 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Chemical and biological labeling is fundamental for the elucidation of the function of proteins within biochemical cellular networks. In particular, fluorescent probes allow detection of molecular interactions, mobility and conformational changes of proteins in live cells with high temporal and spatial resolution. We present a generic method to label proteins in vivo selectively, rapidly (seconds) and reversibly, with small molecular probes that can have a wide variety of properties. These probes comprise a chromophore and a metal-ion-chelating nitrilotriacetate (NTA) moiety, which binds reversibly and specifically to engineered oligohistidine sequences in proteins of interest. We demonstrate the feasibility of the approach by binding NTA-chromophore conjugates to a representative ligand-gated ion channel and G protein-coupled receptor, each containing a polyhistidine sequence. We investigated the ionotropic 5HT(3) serotonin receptor by fluorescence measurements to characterize in vivo the probe-receptor interactions, yielding information on structure and plasma membrane distribution of the receptor.
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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.