Bing Shan, Ph.D.
Affiliations: | 2009 | Stony Brook University, Stony Brook, NY, United States |
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"Bing Shan"Mean distance: 10.58
Parents
Sign in to add mentor| Daniel P. Raleigh | grad student | 2009 | SUNY Stony Brook | |
| (NMR studies of the unfolded states of proteins under native and strongly denaturing conditions.) | ||||
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Publications
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| Meng F, Xin JY, Cao CY, et al. (2016) Seasonal variations in aerosol optical thickness over eastern China determined from VIIRS data and ground measurements International Journal of Remote Sensing. 37: 1868-1880 |
| Xiao S, Patsalo V, Shan B, et al. (2013) Rational modification of protein stability by targeting surface sites leads to complicated results. Proceedings of the National Academy of Sciences of the United States of America. 110: 11337-42 |
| 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 |
| Shan B, Li DW, Brüschweiler-Li L, et al. (2012) Competitive binding between dynamic p53 transactivation subdomains to human MDM2 protein: implications for regulating the p53·MDM2/MDMX interaction. The Journal of Biological Chemistry. 287: 30376-84 |
| Shan B, McClendon S, Rospigliosi C, et al. (2010) The cold denatured state of the C-terminal domain of protein L9 is compact and contains both native and non-native structure. Journal of the American Chemical Society. 132: 4669-77 |
| Meng W, Shan B, Tang Y, et al. (2009) Native like structure in the unfolded state of the villin headpiece helical subdomain, an ultrafast folding protein. Protein Science : a Publication of the Protein Society. 18: 1692-701 |
| Xiao S, Bi Y, Shan B, et al. (2009) Analysis of core packing in a cooperatively folded miniature protein: the ultrafast folding villin headpiece helical subdomain. Biochemistry. 48: 4607-16 |
| Shan B, Eliezer D, Raleigh DP. (2009) The unfolded state of the C-terminal domain of the ribosomal protein L9 contains both native and non-native structure. Biochemistry. 48: 4707-19 |
| Raleigh DP, Shan B, Meng W, et al. (2009) Characterization of the Unfolded State Under Native Conditions: A Missing Piece of the Protein Folding Puzzle Biophysical Journal. 96: 220a |
| Shan B, Bhattacharya S, Eliezer D, et al. (2008) The low-pH unfolded state of the C-terminal domain of the ribosomal protein L9 contains significant secondary structure in the absence of denaturant but is no more compact than the low-pH urea unfolded state. Biochemistry. 47: 9565-73 |