ArticleBiochemistry2011
Specific labeling of threonine methyl groups for NMR studies of protein-nucleic acid complexes.
Article in Biochemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 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
11 citing papers in PubMed, 25 citations in OpenAlex.
- Dynamic sampling of a surveillance state enables DNA proofreading by Cas9.Cell chemical biology · 2025Article
- Bacterial production of site specificJournal of biomolecular NMR · 2017Article
- Determination of ligand binding modes in weak protein-ligand complexes using sparse NMR data.Journal of biomolecular NMR · 2016Article
- Exploiting E. coli auxotrophs for leucine, valine, and threonine specific methyl labeling of large proteins for NMR applications.Journal of biomolecular NMR · 2016Article
- Article
- A 3D time-shared NOESY experiment designed to provide optimal resolution for accurate assignment of NMR distance restraints in large proteins.Journal of biomolecular NMR · 2014Article
- Practical aspects of NMR signal assignment in larger and challenging proteins.Progress in nuclear magnetic resonance spectroscopy · 2014Review
- NMR methods for structural studies of large monomeric and multimeric proteins.Current opinion in structural biology · 2013Review
- Divide and conquer is always best: sensitivity of methyl correlation experiments.Journal of biomolecular NMR · 2013Article
- The quiet renaissance of protein nuclear magnetic resonance.Biochemistry · 2013Review
- Article
Corrections and comments
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
Abstract
Specific (13)C labeling of Thr methyl groups has been accomplished via the growth of a standard laboratory strain of Escherichia coli on [2-(13)C]glycerol in the presence of deuterated isoketovalerate, Ile, and Ala. Diversion of the label from the Thr biosynthetic pathway is suppressed by including Lys, Met, and Ile in the growth medium. This method complements the repertoire of methyl labeling schemes for NMR structural and dynamic studies of proteins and is particularly useful for the study of nucleic acid binding proteins because of the high propensity of Thr residues at protein-DNA and -RNA interfaces.
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What OpenQuestion holds
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.