| Year |
Citation |
Score |
| 2018 |
Stenzoski NE, Luan B, Holehouse AS, Raleigh DP. The Unfolded State of the C-Terminal Domain of L9 Expands at Low but Not at Elevated Temperatures. Biophysical Journal. PMID 30098729 DOI: 10.1016/J.Bpj.2018.07.013 |
0.556 |
|
| 2016 |
Xu Z, Zhang S, Weber JK, Luan B, Zhou R, Li J. Sequential protein unfolding through a carbon nanotube pore. Nanoscale. PMID 26899409 DOI: 10.1039/c6nr00410e |
0.374 |
|
| 2016 |
Luan B, Huynh T, Zhou R. Potential Interference of Protein-Protein Interactions by Graphyne. The Journal of Physical Chemistry. B. PMID 26885561 DOI: 10.1021/acs.jpcb.5b11449 |
0.332 |
|
| 2015 |
Luan B, Huynh T, Li J, Zhou R. Nanomechanics of Protein Unfolding Outside a Generic Nanopore. Acs Nano. PMID 26655061 DOI: 10.1021/acsnano.5b04557 |
0.337 |
|
| 2014 |
Lahiri T, Luan B, Raleigh DP, Boon EM. 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. PMID 24628400 DOI: 10.1021/Bi401597M |
0.478 |
|
| 2014 |
Luan B, Lyle N, Pappu RV, Raleigh DP. Denatured state ensembles with the same radii of gyration can form significantly different long-range contacts. Biochemistry. 53: 39-47. PMID 24280003 DOI: 10.1021/Bi4008337 |
0.625 |
|
| 2013 |
Meng W, Luan B, Lyle N, Pappu RV, Raleigh DP. 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. PMID 23480024 DOI: 10.1021/Bi301667U |
0.656 |
|
| 2013 |
Luan B, Shan B, Baiz C, Tokmakoff A, Raleigh DP. Cooperative cold denaturation: the case of the C-terminal domain of ribosomal protein L9. Biochemistry. 52: 2402-9. PMID 23461364 DOI: 10.1021/Bi3016789 |
0.642 |
|
| 2013 |
Meng W, Lyle N, Luan B, Raleigh DP, Pappu RV. 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. PMID 23341588 DOI: 10.1073/Pnas.1216979110 |
0.625 |
|
| 2012 |
Patsalo V, Yondola MA, Luan B, Shoshani I, Kisker C, Green DF, Raleigh DP, Hearing P. 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. PMID 22573317 DOI: 10.1074/Jbc.M112.344234 |
0.528 |
|
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