ArticleJournal of biomolecular NMR2021
Toho-1 β-lactamase: backbone chemical shift assignments and changes in dynamics upon binding with avibactam.
Article in Journal of biomolecular NMR, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 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
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Who cites it
6 citing papers in PubMed.
- NMR crystallography reveals active-site protonation states of Toho-1 β-lactamase in complex with avibactam.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Dynamic signature of activity-stability tradeoff in lactamase evolution.Nature communications · 2026Article
- Backbone assignment of a 28.5 kDa class A extended spectrum β-lactamase by high-field, carbon-detected solid-state NMR.Biomolecular NMR assignments · 2025Article
- Ultrahigh-resolution solid-state NMR for high-molecular weight proteins on GHz-class spectrometers.Science advances · 2025Article
- Drug Discovery in the Field of β-Lactams: An Academic Perspective.Antibiotics (Basel, Switzerland) · 2024Review
- Slow Protein Dynamics Elicits New Enzymatic Functions by Means of Epistatic Interactions.Molecular biology and evolution · 2022Article
Corrections and comments
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Authors and funding
6 authors.
Funding
Abstract
Backbone chemical shift assignments for the Toho-1 β-lactamase (263 amino acids, 28.9 kDa) are reported based on triple resonance solution-state NMR experiments performed on a uniformly
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Registered trials
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