ArticleProceedings of the National Academy of Sciences of the United States of America2015
Is pressure-induced signal loss in NMR spectra for the Leu99Ala cavity mutant of T4 lysozyme due to unfolding?
Article in Proceedings of the National Academy of Sciences of the United States of America, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 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
5 citing papers in PubMed.
- How internal cavities destabilize a protein.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- Practical aspects of high-pressure NMR spectroscopy and its applications in protein biophysics and structural biology.Methods (San Diego, Calif.) · 2018Article
- Predicting Binding Free Energies: Frontiers and Benchmarks.Annual review of biophysics · 2017Review
- Structure-relaxation mechanism for the response of T4 lysozyme cavity mutants to hydrostatic pressure.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- Reply to Kitahara and Mulder: An ensemble view of protein stability best explains pressure effects in a T4 lysozyme cavity mutant.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
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Registered trials
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