ArticleJournal of biomolecular NMR2019
Selective isotope labeling for NMR structure determination of proteins in complex with unlabeled ligands.
Article in Journal of biomolecular NMR, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 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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Who cites it
3 citing papers in PubMed.
- Segmental and site-specific isotope labelling strategies for structural analysis of posttranslationally modified proteins.RSC chemical biology · 2021Review
- Applications of Solution NMR in Drug Discovery.Molecules (Basel, Switzerland) · 2021Review
- Deciphering protein post-translational modifications using chemical biology tools.Nature reviews. Chemistry · 2020Review
Corrections and comments
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Authors and funding
5 authors.
Funding
Abstract
The physiological role of proteins is frequently linked to interactions with non-protein ligands or posttranslational modifications. Structural characterization of these complexes or modified proteins by NMR may be difficult as the ligands are usually not available in an isotope-labeled form and NMR spectra may suffer from signal overlap. Here, we present an optimized approach that uses specific NMR isotope-labeling schemes for overcoming both hurdles. This approach enabled the high-resolution structure determination of the farnesylated C-terminal domain of the peroxisomal protein PEX19. The approach combines specific
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Registered trials
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