A general method for the covalent labeling of fusion proteins with small molecules in vivo
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Summary
A general method for the covalent labeling of fusion proteins in vivo that complements existing methods for noncovalentlabeling of proteins and that may open up new ways of studying proteins in living cells is described.
- Type
- article
- Published
- 2003-01-01
- Cited by
- 1,783
- References
- 16
- Access
- Open access
- OpenAlex
- https://openalex.org/W2016036293
- Semantic Scholar
- https://api.semanticscholar.org/CorpusID:1051666
Keywords
Fusion protein, Function (biology), Green fluorescent protein, Covalent bond, Small molecule
References
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- Synthesis and Applications of Chemical Probes for Human O6‐Alkylguanine‐DNA Alkyltransferase
- New biarsenical ligands and tetracysteine motifs for protein labeling in vitro and in vivo: synthesis and biological applications.
- A novel genetic system to detect proteinprotein interactions
- Split ubiquitin as a sensor of protein interactions in vivo.
- A plasmid expression system for quantitative in vivo biotinylation of thioredoxin fusion proteins in Escherichia coli.
- A short amino acid sequence able to specify nuclear location.
- Role of codon 160 in the sensitivity of human O6-alkylguanine-DNA alkyltransferase to O6-benzylguanine.
- Receptor-mediated Targeting of Fluorescent Probes in Living Cells*
- Multicolor and Electron Microscopic Imaging of Connexin Trafficking
- Transfection and expression of human O6-methylguanine-DNA methyltransferase (MGMT) cDNA in Chinese hamster cells: the role of MGMT in protection against the genotoxic effects of alkylating agents.
- Intracellular localization and intercellular heterogeneity of the human DNA repair protein O6-methylguanine-DNA methyltransferase
- Specific covalent labeling of recombinant protein molecules inside live cells.
- Organelle pH studies using targeted avidin and fluorescein-biotin.
- GREEN FLUORESCENT PROTEIN
Cited by
- Using peptide loop insertion mutagenesis for the evolution of proteins.
- A general approach for chemical labeling and rapid, spatially controlled protein inactivation.
- New methodologies for measuring protein interactions in vivo and in vitro.
- Remodelling epithelial tubes through cell rearrangements: from cells to molecules
- An improved bioluminescence resonance energy transfer strategy for imaging intracellular events in single cells and living subjects.
- Protein C-Terminal Labeling and Biotinylation Using Synthetic Peptide and Split-Intein
- Fluorogenic Dendrons with Multiple Donor Chromophores as Bright Genetically Targeted and Activated Probes
- Caenorhabditis elegans Galectins LEC-6 and LEC-10 Interact with Similar Glycoconjugates in the Intestine
- The controlled display of biomolecules on nanoparticles: a challenge suited to bioorthogonal chemistry.
- Control of a tyrosyl radical mediated protein cross-linking reaction by electrostatic interaction.
- Development of a simple method for protein conjugation by copper-free click reaction and its application to antibody-free Western blot analysis.
- Selection of a T7 promoter mutant with enhanced in vitro activity by a novel multi-copy bead display approach for in vitro evolution
- Preparation of covalently linked complexes between DNA and O(6)-alkylguanine-DNA alkyltransferase using interstrand cross-linked DNA.
- Protein engineering for directed immobilization.
- Enzymatic “Click” Ligation: Selective Cysteine Modification in Polypeptides Enabled by Promiscuous Glutathione S-Transferase
- DIVERSE System: De Novo Creation of Peptide Tags for Non-enzymatic Covalent Labeling by In Vitro Evolution for Protein Imaging Inside Living Cells.
- HTS-compatible FRET-based conformational sensors clarify membrane receptor activation.
- Optimized labeling of membrane proteins for applications to super-resolution imaging in confined cellular environments using monomeric streptavidin
- Analysis of Ciliary Membrane Protein Dynamics Using SNAP Technology
- Shedding light on metabotropic glutamate receptors using optogenetics and photopharmacology
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