科研成果 by Year: 2010

2010
Wang Y, Lai L. Modeling the intracellular dynamics for Vif-APO mediated HIV-1 virus infection. Chinese Science Bulletin. 2010;(22):2329-2340.
Wei P, Li C-M, Zhou L, Liu Y, Lai L-H. Substrate binding and homo-dimerization of SARS 3CL proteinase are mutual allosteric effectors. Wuli Huaxue Xuebao/ Acta Physico - Chimica Sinica. 2010;(4):1093-1098.
He S, Lai L-H. Recent advances in RNA riboswitch. Progress in Biochemistry and Biophysics. 2010;(1):7-13.
Cao A-N, Wang W-X, Yuwen T-R, Deng W, Lai L-H. Inhibition of amyloid fibrillization and dissociation of matured amyloid fibrils by Mj HSP16.5. Wuli Huaxue Xuebao/ Acta Physico - Chimica Sinica. 2010;(7):2015-2020.
Bai H-J, Lai L-H. Protein-protein interactions: Interface analysis, binding free energy calculation and interaction design. Wuli Huaxue Xuebao/ Acta Physico - Chimica Sinica. 2010;(7):1988-1997.
Wei D, Zheng H, Su N, Deng M, Lai L. Binding energy landscape analysis helps to discriminate true hits from high-scoring decoys in virtual screening. Journal of Chemical Information and Modeling [Internet]. 2010;(10):1855-1864. 访问链接
Qi Y, Huang Y, Liang H, Liu Z, Lai L. Folding simulations of a de Novo designed protein with a βαβ fold. Biophysical Journal [Internet]. 2010;(2):321-329. 访问链接
Jiang X, Zhou L, Wu Y, Wei D, Sun C, Jia J, Liu Y, Lai L. Modulating the substrate specificity of LTA4H aminopeptidase by using chemical compounds and small-molecule-guided mutagenesis. ChemBioChem [Internet]. 2010;(8):1120-1128. 访问链接
Li C, Qi Y, Teng X, Yang Z, Wei P, Zhang C, Tan L, Zhou L, Liu Y, Lai L. Maturation mechanism of severe acute respiratory syndrome (SARS) coronavirus 3C-like proteinase. Journal of Biological Chemistry [Internet]. 2010;(36):28134-28140. 访问链接
Gao X, Wang J, Yu D-Q, Bian F, Xie B-B, Chen X-L, Zhou B-C, Lai L-H, Wang Z-X, Wu J-W, et al. Structural basis for the autoprocessing of zinc metalloproteases in the thermolysin family. Proceedings of the National Academy of Sciences of the United States of America [Internet]. 2010;(41):17569-17574. 访问链接