| Year |
Citation |
Score |
| 2016 |
Meng F, Xin JY, Cao CY, Shao X, Shan BY, Xiao QF. Seasonal variations in aerosol optical thickness over eastern China determined from VIIRS data and ground measurements International Journal of Remote Sensing. 37: 1868-1880. DOI: 10.1080/01431161.2016.1163750 |
0.435 |
|
| 2013 |
Xiao S, Patsalo V, Shan B, Bi Y, Green DF, Raleigh DP. 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. PMID 23798426 DOI: 10.1073/Pnas.1222245110 |
0.672 |
|
| 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 |
0.705 |
|
| 2012 |
Shan B, Li DW, Brüschweiler-Li L, Brüschweiler R. 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. PMID 22807444 DOI: 10.1074/Jbc.M112.369793 |
0.341 |
|
| 2010 |
Shan B, McClendon S, Rospigliosi C, Eliezer D, Raleigh DP. 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. PMID 20225821 DOI: 10.1021/Ja908104S |
0.702 |
|
| 2009 |
Meng W, Shan B, Tang Y, Raleigh DP. 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. PMID 19598233 DOI: 10.1002/Pro.152 |
0.724 |
|
| 2009 |
Xiao S, Bi Y, Shan B, Raleigh DP. Analysis of core packing in a cooperatively folded miniature protein: the ultrafast folding villin headpiece helical subdomain. Biochemistry. 48: 4607-16. PMID 19354264 DOI: 10.1021/Bi8021763 |
0.657 |
|
| 2009 |
Shan B, Eliezer D, Raleigh DP. The unfolded state of the C-terminal domain of the ribosomal protein L9 contains both native and non-native structure. Biochemistry. 48: 4707-19. PMID 19301913 DOI: 10.1021/Bi802299J |
0.667 |
|
| 2009 |
Raleigh DP, Shan B, Meng W, Cho J, Taskent H. Characterization of the Unfolded State Under Native Conditions: A Missing Piece of the Protein Folding Puzzle Biophysical Journal. 96: 220a. DOI: 10.1016/J.Bpj.2008.12.1921 |
0.73 |
|
| 2008 |
Shan B, Bhattacharya S, Eliezer D, Raleigh DP. 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. PMID 18707127 DOI: 10.1021/Bi8006862 |
0.667 |
|
| 2008 |
Shan B, Bhattacharya S, Eliezer D, Raleigh D. Backbone and 13C and 1H assignments for acid unfolded state and urea unfolded state of CTL9 Journal of Back and Musculoskeletal Rehabilitation. DOI: 10.13018/Bmr15883 |
0.601 |
|
| 2007 |
Bi Y, Cho JH, Kim EY, Shan B, Schindelin H, Raleigh DP. Rational design, structural and thermodynamic characterization of a hyperstable variant of the villin headpiece helical subdomain. Biochemistry. 46: 7497-505. PMID 17536785 DOI: 10.1021/Bi6026314 |
0.663 |
|
| 2007 |
Li Y, Shan B, Raleigh DP. The cold denatured state is compact but expands at low temperatures: hydrodynamic properties of the cold denatured state of the C-terminal domain of L9. Journal of Molecular Biology. 368: 256-62. PMID 17337003 DOI: 10.1016/J.Jmb.2007.02.011 |
0.645 |
|
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