1. | H. Wang, S. Wang, C. Li, H. Li, Y. Mao, W. Liu, C. Xu*, D. Long* (2017) Probing transient release of membrane-sequestered tyrosine-based signaling motif by solution NMR spectroscopy. J. Phys. Chem. Lett. 8:3765-3769 |
2. | Y. Mao, H. Yao, H. Wang, P. Cheng, D. Long* (2016) Microsecond timescale dynamics of GDP-bound Ras underlies the formation of novel inhibitor-binding pockets. Angew. Chem. Int. Ed. 55:15629-15632 |
3. | D. Long,* F. Delaglio, A. Sekhar, L. E. Kay* (2015) Probing invisible, excited protein states by non-uniformly sampled pseudo-4D CEST spectroscopy. Angew. Chem. Int. Ed. 54:10507-10511 |
4. | D. Long, A. Sekhar, L. E. Kay (2014) Triple resonance-based 13Cα and 13Cβ CEST experiments for studies of ms timescale dynamics in proteins. J. Biomol. NMR 60:203-208 |
5. | D. Long, G. Bouvignies, L. E. Kay (2014) Measuring hydrogen exchange rates in invisible protein excited states. Proc. Natl. Acad. Sci. U.S.A. 111:8820-8825 (Recommended by Faculty of 1000) |
6. | D. Long, C. B. Marshall, G. Bouvignies, M. T. Mazhab-Jafari, M. J. Smith, M. Ikura, L. E. Kay. (2013) A comparative CEST NMR study of slow conformational dynamics of small GTPases complexed with GTP and GTP analogues. Angew. Chem. Int. Ed. 52:10771-10774 (Recommended by Faculty of 1000) |
7. | H. Sun, D. Long, R. Brüschweiler, V. Tugarinov. (2013) Carbon relaxation in 13Cα-Hα and 13Cα-Dα spin pairs as a probe of backbone dynamics in proteins. J. Phys. Chem. B 117:1308-1320 |
8. | D. Long, R. Brüschweiler. (2013) Directional selection precedes conformational selection in ubiquitin-UIM binding. Angew. Chem. Int. Ed. 52: 3709-3711 |
9. | D. Long, R. Brüschweiler. (2012) Structural and entropic allosteric signal transduction strength via correlated motions. J. Phys. Chem. Lett. 3:1722-1726 |
10. | D. Long, R. Brüschweiler. (2011) Atomistic kinetic model for population shift and allostery in biomolecules. J. Am. Chem. Soc. 133:18999-19005 |
11. | D. Long, D.W. Li, K. Walter, C. Griesinger, R. Brüschweiler. (2011) Toward a predictive understanding of slow methyl group dynamics in proteins. Biophys. J. 101:910-915 |
12. | D. Long, R. Brüschweiler. (2011) In silico elucidation of the recognition dynamics of ubiquitin. PLoS Comput. Biol. 7: e1002035 |