The DOI matches its Crossref record; 3 of the 3 references it cites were found in a registry or an index.
Solution NMR-derived global fold of a monomeric 82-kDa enzyme
Open accessAbstract
The size of proteins that can be studied by solution NMR spectroscopy has increased significantly because of recent developments in methodology. Important experiments include those that make use of approaches that increase the lifetimes of NMR signals or that define the orientation of internuclear bond vectors with respect to a common molecular frame. The advances in NMR techniques are strongly coupled to isotope labeling methods that increase sensitivity and reduce the complexity of NMR spectra. We show that these developments can be exploited in structural studies of high-molecular-weight, single-polypeptide proteins, and we present the solution global fold of the monomeric 723-residue (82-kDa) enzyme malate synthase G from Escherichia coli , which has been extensively characterized by NMR in the past several years.
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AQUA and PROCHECK-NMR: Programs for checking the quality of protein structures solved by NMR
Laskowski, R., Rullmann, J. A., MacArthur, M., Kaptein, R., & Thornton, J. (1996) · Journal of Biomolecular NMR · doi:10.1007/bf00228148 · Cited by 5,502
Protein backbone angle restraints from searching a database for chemical shift and sequence homology
Cornilescu, G., Delaglio, F., & Bax, A. (1999) · Journal of Biomolecular NMR · doi:10.1023/a:1008392405740 · Cited by 2,957
The glyoxylate cycle is required for fungal virulence
Lorenz, M. C., & Fink, G. R. (2001) · Nature · doi:10.1038/35083594 · Cited by 745
Cited by
An NMR Perspective on Enzyme Dynamics
Boehr, D. D., Dyson, H. J., & Wright, P. E. (2006) · Chemical Reviews · doi:10.1021/cr050312q · Cited by 458
Major roles of isocitrate lyase and malate synthase in bacterial and fungal pathogenesis
Dunn, M. F., Ramírez-Trujillo, J. A., & Hernández-Lucas, I. (2009) · Microbiology · doi:10.1099/mic.0.030858-0 · Cited by 304
Automatic structure-based NMR methyl resonance assignment in large proteins
Pritišanac, I., Würz, J. M., Alderson, T. R., & Güntert, P. (2019) · Nature Communications · doi:10.1038/s41467-019-12837-8 · Cited by 46
Progress toward automated methyl assignments for methyl-TROSY applications
Clay, M. C., Saleh, T., Kamatham, S., Rossi, P., & Kalodimos, C. G. (2022) · Structure · doi:10.1016/j.str.2021.11.009 · Cited by 9
Cryo-EM reveals the structure and dynamics of a 723-residue malate synthase G
Ho, M.-R., Wu, Y.-M., Lu, Y.-C., Ko, T.-P., & Wu, K.-P. (2023) · Journal of Structural Biology · doi:10.1016/j.jsb.2023.107958 · Cited by 8
Metadata
- Authors
- Tugarinov, V., Choy, W.-Y., Orekhov, V. Y., & Kay, L. E.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 2005-01-06
- Volume
- 102
- Issue
- 3
- Pages
- 622-627
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W2036664878
- Cited by
- 223
- References
- 3
- FWCI
- 7.37
- Type
- journal article
- Language
- en
- Open access
- green
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- Tugarinov, V., Choy, W.-Y., Orekhov, V. Y., & Kay, L. E. (2005). Solution NMR-derived global fold of a monomeric 82-kDa enzyme. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.0407792102
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