The DOI matches its Crossref record; 40 of the 40 references it cites were found in a registry or an index.
A Transient and Low-Populated Protein-Folding Intermediate at Atomic Resolution
Abstract
Transient Protein Conformations: Transient conformations are important to protein function; however, detecting and characterizing these states is technically challenging. Korzhnev et al. (p. 1312 ; see the Perspective by Al-Hashimi ) combined recently developed methods to determine the three-dimensional atomic-resolution structure of a transient intermediate of a four-helix bundle protein domain. The intermediate formed rapidly but, owing to structural peculiarities, slowly rearranged into its native state. The methods can be applied not only to folding intermediates but also to excited states important for protein function.
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Cites
TALOS+: a hybrid method for predicting protein backbone torsion angles from NMR chemical shifts
Shen, Y., Delaglio, F., Cornilescu, G., & Bax, A. (2009) · Journal of Biomolecular NMR · doi:10.1007/s10858-009-9333-z · Cited by 2,516
Structure and Mechanism in Protein Science: A Guide to Enzyme Catalysis and Protein Folding
Fersht, A. (2017) · Series in Structural Biology · doi:10.1142/10574 · Cited by 2,039
Self-citationSattler, M. (1999) · Progress in Nuclear Magnetic Resonance Spectroscopy · doi:10.1016/s0079-6565(98)00025-9 · Cited by 1,722
Tjandra, N., & Bax, A. (1997) · Science · doi:10.1126/science.278.5340.1111 · Cited by 1,719
Macromolecular Modeling with Rosetta
Das, R., & Baker, D. (2008) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.77.062906.171838 · Cited by 989
Palmer, A. G., Kroenke, C. D., & Patrick Loria, J. (2001) · Methods in Enzymology · doi:10.1016/s0076-6879(01)39315-1 · Cited by 938
Protein Folding: A Perspective from Theory and Experiment
Dobson, C. M., Šali, A., & Karplus, M. (1998) · Angewandte Chemie International Edition · doi:10.1002/(sici)1521-3773(19980420)37:7<868::aid-anie868>3.0.co;2-h · Cited by 869
Consistent blind protein structure generation from NMR chemical shift data
Shen, Y., Lange, O., Delaglio, F., Rossi, P., Aramini, J. M., Liu, G., Eletsky, A., Wu, Y., Singarapu, K. K., Lemak, A., et al. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0800256105 · Cited by 855
Mapping the transition state and pathway of protein folding by protein engineering
Matouschek, A., Kellis, J. T., Serrano, L., & Fersht, A. R. (1989) · Nature · doi:10.1038/340122a0 · Cited by 703
Self-citationLoria, J. P., Rance, M., & Palmer, A. G. (1999) · Journal of the American Chemical Society · doi:10.1021/ja983961a · Cited by 679
Cited by
Studying “Invisible” Excited Protein States in Slow Exchange with a Major State Conformation
Vallurupalli, P., Bouvignies, G., & Kay, L. E. (2012) · Journal of the American Chemical Society · doi:10.1021/ja3001419 · Cited by 526
Self-citationStructure of an Intermediate State in Protein Folding and Aggregation
Neudecker, P., Robustelli, P., Cavalli, A., Walsh, P., Lundström, P., Zarrine-Afsar, A., Sharpe, S., Vendruscolo, M., & Kay, L. E. (2012) · Science · doi:10.1126/science.1214203 · Cited by 398
Self-citationTransient Hoogsteen base pairs in canonical duplex DNA
Nikolova, E. N., Kim, E., Wise, A. A., O’Brien, P. J., Andricioaei, I., & Al-Hashimi, H. M. (2011) · Nature · doi:10.1038/nature09775 · Cited by 344
Chemical exchange in biomacromolecules: Past, present, and future
Palmer, A. G. (2014) · Journal of Magnetic Resonance · doi:10.1016/j.jmr.2014.01.008 · Cited by 263
Nonnative SOD1 trimer is toxic to motor neurons in a model of amyotrophic lateral sclerosis
Proctor, E. A., Fee, L., Tao, Y., Redler, R. L., Fay, J. M., Zhang, Y., Lv, Z., Mercer, I. P., Deshmukh, M., Lyubchenko, Y. L., et al. (2016) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1516725113 · Cited by 131
Metadata
- Authors
- Korzhnev, D. M., Religa, T. L., Banachewicz, W., Fersht, A. R., & Kay, L. E.
- Venue
- Science
- Published
- 2010-09-10
- Volume
- 329
- Issue
- 5997
- Pages
- 1312-1316
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W2168875869
- Cited by
- 305
- References
- 40
- FWCI
- 16.07
- Type
- journal article
- Language
- en
- Open access
- closed
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