Bowu Luan, Ph.D.
Affiliations: | 2014 | Chemistry | Stony Brook University, Stony Brook, NY, United States |
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Parents
Sign in to add mentor| Daniel P. Raleigh | grad student | 2014 | SUNY Stony Brook | |
| (The Other Half of the Protein Folding Equation Characterization of the Protein Denatured State Ensemble (DSE): The Case of C-terminal Domain of the Ribosomal Protein L9 (CTL9).) | ||||
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| Stenzoski NE, Luan B, Holehouse AS, et al. (2018) The Unfolded State of the C-Terminal Domain of L9 Expands at Low but Not at Elevated Temperatures. Biophysical Journal |
| Xu Z, Zhang S, Weber JK, et al. (2016) Sequential protein unfolding through a carbon nanotube pore. Nanoscale |
| Luan B, Huynh T, Zhou R. (2016) Potential Interference of Protein-Protein Interactions by Graphyne. The Journal of Physical Chemistry. B |
| Luan B, Huynh T, Li J, et al. (2015) Nanomechanics of Protein Unfolding Outside a Generic Nanopore. Acs Nano |
| Lahiri T, Luan B, Raleigh DP, et al. (2014) A structural basis for the regulation of an H-NOX-associated cyclic-di-GMP synthase/phosphodiesterase enzyme by nitric oxide-bound H-NOX. Biochemistry. 53: 2126-35 |
| Luan B, Lyle N, Pappu RV, et al. (2014) Denatured state ensembles with the same radii of gyration can form significantly different long-range contacts. Biochemistry. 53: 39-47 |
| Meng W, Luan B, Lyle N, et al. (2013) The denatured state ensemble contains significant local and long-range structure under native conditions: analysis of the N-terminal domain of ribosomal protein L9. Biochemistry. 52: 2662-71 |
| Luan B, Shan B, Baiz C, et al. (2013) Cooperative cold denaturation: the case of the C-terminal domain of ribosomal protein L9. Biochemistry. 52: 2402-9 |
| Meng W, Lyle N, Luan B, et al. (2013) Experiments and simulations show how long-range contacts can form in expanded unfolded proteins with negligible secondary structure. Proceedings of the National Academy of Sciences of the United States of America. 110: 2123-8 |
| Patsalo V, Yondola MA, Luan B, et al. (2012) Biophysical and functional analyses suggest that adenovirus E4-ORF3 protein requires higher-order multimerization to function against promyelocytic leukemia protein nuclear bodies. The Journal of Biological Chemistry. 287: 22573-83 |