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Automated NMR Structure Calculation With CYANA
Abstract
This chapter gives an introduction to automated nuclear magnetic resonance (NMR) structure calculation with the program CYANA. Given a sufficiently complete list of assigned chemical shifts and one or several lists of cross-peak positions and columns from two-, three-, or four-dimensional nuclear Overhauser effect spectroscopy (NOESY) spectra, the assignment of the NOESY cross-peaks and the three-dimensional structure of the protein in solution can be calculated automatically with CYANA.
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Allen, M. P., & Tildesley, D. J. (2017) · doi:10.1093/oso/9780198803195.001.0001 · Cited by 20,945
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Tang, J., Cho, N. W., Cui, G., Manion, E. M., Shanbhag, N. M., Botuyan, M. V., Mer, G., & Greenberg, R. A. (2013) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.2499 · Cited by 521
Structural basis for protein antiaggregation activity of the trigger factor chaperone.
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Chen, J., Li, Q., & Wang, J. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1106420108 · Cited by 283
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Jordan, J. B., Poppe, L., Haniu, M., Arvedson, T., Syed, R., Li, V., Kohno, H., Kim, H., Schnier, P. D., Harvey, T. S., et al. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.017764 · Cited by 214
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Eidahl, J. O., Crowe, B. L., North, J. A., McKee, C. J., Shkriabai, N., Feng, L., Plumb, M., Graham, R. L., Gorelick, R. J., Hess, S., et al. (2013) · Nucleic Acids Research · doi:10.1093/nar/gkt074 · Cited by 207
Xue, J., Ray, R., Singer, D., Böhme, D., Burz, D. S., Rai, V., Hoffmann, R., & Shekhtman, A. (2014) · Biochemistry · doi:10.1021/bi500046t · Cited by 186
Cabrales Fontela, Y., Kadavath, H., Biernat, J., Riedel, D., Mandelkow, E., & Zweckstetter, M. (2017) · Nature Communications · doi:10.1038/s41467-017-02230-8 · Cited by 148
Buck-Koehntop, B. A., Stanfield, R. L., Ekiert, D. C., Martinez-Yamout, M. A., Dyson, H. J., Wilson, I. A., & Wright, P. E. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1213726109 · Cited by 128
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Weiss, A., Murdoch, C. C., Edmonds, K. A., Jordan, M. R., Monteith, A. J., Perera, Y. R., Rodríguez Nassif, A. M., Petoletti, A. M., Beavers, W. N., Munneke, M. J., et al. (2022) · Cell · doi:10.1016/j.cell.2022.04.011 · Cited by 113
Banci, L., Bertini, I., Cantini, F., Rosenzweig, A. C., & Yatsunyk, L. A. (2008) · Biochemistry · doi:10.1021/bi8004736 · Cited by 105
Chan, L. Y., Zhang, V. M., Huang, Y., Waters, N. C., Bansal, P. S., Craik, D. J., & Daly, N. L. (2013) · ChemBioChem · doi:10.1002/cbic.201300034 · Cited by 88
Millard, C. J., Ludeman, J. P., Canals, M., Bridgford, J. L., Hinds, M. G., Clayton, D. J., Christopoulos, A., Payne, R. J., & Stone, M. J. (2014) · Structure · doi:10.1016/j.str.2014.08.023 · Cited by 75
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Lemak, A., Yee, A., Wu, H., Yap, D., Zeng, H., Dombrovski, L., Houliston, S., Aparicio, S., & Arrowsmith, C. H. (2013) · PLoS ONE · doi:10.1371/journal.pone.0077020 · Cited by 36
Koveal, D., Schuh-Nuhfer, N., Ritt, D., Page, R., Morrison, D. K., & Peti, W. (2012) · Science Signaling · doi:10.1126/scisignal.2003289 · Cited by 36
Dorn, G., Gmeiner, C., de Vries, T., Dedic, E., Novakovic, M., Damberger, F. F., Maris, C., Finol, E., Sarnowski, C. P., Kohlbrecher, J., et al. (2023) · Nature Communications · doi:10.1038/s41467-023-42012-z · Cited by 27
Large-scale discovery, analysis and design of protein energy landscapes
Ferrari, Á. J. R., Dixit, S. M., Thibeault, J., Garcia, M., Houliston, S., Ludwig, R. W., Notin, P., Phoumyvong, C. M., Martell, C. M., Jung, M. D., et al. (2026) · Nature · doi:10.1038/s41586-026-10465-z · Cited by 22
Low, K. E., Gheorghita, A. A., Tammam, S. D., Whitfield, G. B., Li, Y. E., Riley, L. M., Weadge, J. T., Caldwell, S. J., Chong, P. A., Walvoort, M. T. C., et al. (2023) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2023.105314 · Cited by 11
Lesovoy, D., Roshchin, K., Sala, B. M., Sandalova, T., Achour, A., Agback, T., Orekhov, V., & Agback, P. (2025) · doi:10.1101/2025.02.07.637034 · Cited by 6
Godwin, J., Djami-Tchatchou, A. T., Velivelli, S. L. S., Tetorya, M., Kalunke, R., Pokhrel, A., Zhou, M., Buchko, G. W., Czymmek, K. J., & Shah, D. M. (2024) · PLOS Pathogens · doi:10.1371/journal.ppat.1012745 · Cited by 6
Brown, J. B., Lee, M. A., & Smith, A. T. (2022) · JBIC Journal of Biological Inorganic Chemistry · doi:10.1007/s00775-022-01945-4 · Cited by 5
Shah, A., Patel, H., Kanjarpane, A., Summers, M. F., & Marchant, J. (2025) · Journal of the American Chemical Society · doi:10.1021/jacs.4c17823 · Cited by 3
Fowler, N. J., Albalwi, M. F., Lee, S., Hounslow, A. M., & Williamson, M. P. (2022) · doi:10.1101/2022.08.29.505644
Metadata
- Authors
- Güntert, P.
- Venue
- Protein NMR Techniques
- Publisher
- Humana Press
- Published
- 2004-08-18
- Volume
- 278
- Pages
- 353-378
- OpenAlex
- W199186236
- Cited by
- 1,351
- References
- 1
- FWCI
- 43.86
- Type
- book chapter
- Language
- en
- Open access
- closed
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