ReviewJournal of biomolecular NMR2010
Site-specific labeling of proteins with NMR-active unnatural amino acids.
Review in Journal of biomolecular NMR, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.
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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
34 citing papers in PubMed, 94 citations in OpenAlex.
- Noncanonical Amino Acid Tools and Their Application to Membrane Protein Studies.Chemical reviews · 2024Review
- Noncanonical Amino Acids in Biocatalysis.Chemical reviews · 2024Review
- GPCR structural characterization by NMR spectroscopy in solution.Acta biochimica et biophysica Sinica · 2022Review
- Paramagnetic Chemical Probes for Studying Biological Macromolecules.Chemical reviews · 2022Review
- FRET sensors reveal the retinal entry pathway in the G protein-coupled receptor rhodopsin.iScience · 2022Article
- Cell Engineering and Cultivation of Chinese Hamster Ovary Cells for the Development of Orthogonal Eukaryotic Cell-free Translation Systems.Frontiers in molecular biosciences · 2022Article
- Site-selective generation of lanthanoid binding sites on proteins using 4-fluoro-2,6-dicyanopyridine.Magnetic resonance (Gottingen, Germany) · 2022Article
- Completing the canvas: advances and challenges for DNA-PAINT super-resolution imaging.Trends in biochemical sciences · 2021Review
- Segmental and site-specific isotope labelling strategies for structural analysis of posttranslationally modified proteins.RSC chemical biology · 2021Review
- Real-time nuclear magnetic resonance spectroscopy in the study of biomolecular kinetics and dynamics.Magnetic resonance (Gottingen, Germany) · 2021Review
- Phosphoserine for the generation of lanthanide-binding sites on proteins for paramagnetic nuclear magnetic resonance spectroscopy.Magnetic resonance (Gottingen, Germany) · 2021Article
- Paramagnetic NMR in drug discovery.Journal of biomolecular NMR · 2020Review
- Current NMR Techniques for Structure-Based Drug Discovery.Molecules (Basel, Switzerland) · 2018Review
- Peptide and Protein Dynamics and Low-Temperature/DNP Magic Angle Spinning NMR.The journal of physical chemistry. B · 2017Article
- A molecular engineering toolbox for the structural biologist.Quarterly reviews of biophysics · 2017Review
- Azidoethoxyphenylalanine as a Vibrational Reporter and Click Chemistry Partner in Proteins.Chemistry (Weinheim an der Bergstrasse, Germany) · 2015Article
- In-Membrane Chemical Modification (IMCM) for Site-Specific Chromophore Labeling of GPCRs.Angewandte Chemie (International ed. in English) · 2015Article
- Paramagnetic NMR probes for characterization of the dynamic conformations and interactions of oligosaccharides.Glycoconjugate journal · 2015Review
- Paramagnetic relaxation enhancement of membrane proteins by incorporation of the metal-chelating unnatural amino acid 2-amino-3-(8-hydroxyquinolin-3-yl)propanoic acid (HQA).Journal of biomolecular NMR · 2015Article
- Therapeutic applications of an expanded genetic code.Chembiochem : a European journal of chemical biology · 2014Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
9 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
A large number of amino acids other than the canonical amino acids can now be easily incorporated in vivo into proteins at genetically encoded positions. The technology requires an orthogonal tRNA/aminoacyl-tRNA synthetase pair specific for the unnatural amino acid that is added to the media while a TAG amber or frame shift codon specifies the incorporation site in the protein to be studied. These unnatural amino acids can be isotopically labeled and provide unique opportunities for site-specific labeling of proteins for NMR studies. In this perspective, we discuss these opportunities including new photocaged unnatural amino acids, outline usage of metal chelating and spin-labeled unnatural amino acids and expand the approach to in-cell NMR experiments.
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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.