Liu, P., Wei, Y., Fan, Y., Li, R., Liu, Y., Wang, G., … Qin, W. (2018). Altered brain structure in women with premenstrual syndrome. Journal of Affective Disorders, 229, 239-246. https://doi.org/10.1016/j.jad.2017.12.075 (Original work published 2018)

Hecht, M., Das, A., Go, A., Bradley, L., & Wei, Y. (2004). De novo proteins from designed combinatorial libraries. Protein Science : A Publication of the Protein Society, 13(7), 1711-23. https://doi.org/10.1110/ps.04690804

Wang, Z., Ye, C., Zhang, X., & Wei, Y. (2015). Cysteine residue is not essential for CPM protein thermal-stability assay. Analytical and Bioanalytical Chemistry, 407(13), 3683-91. https://doi.org/10.1007/s00216-015-8587-4

Zhong, M., Ferrell, B., Lu, W., Chai, Q., & Wei, Y. (2013). Insights into the function and structural flexibility of the periplasmic molecular chaperone SurA. Journal of Bacteriology, 195(5), 1061-7. https://doi.org/10.1128/JB.01143-12

Yu, L., Lu, W., Ye, C., Wang, Z., Zhong, M., Chai, Q., … Wei, Y. (2013). Role of a conserved residue R780 in Escherichia coli multidrug transporter AcrB. Biochemistry, 52(39), 6790-6. https://doi.org/10.1021/bi400452v (Original work published 2013)

Lu, W., Zhong, M., Chai, Q., Wang, Z., Yu, L., & Wei, Y. Functional relevance of AcrB Trimerization in pump assembly and substrate binding. PloS One, 9(2), e89143. https://doi.org/10.1371/journal.pone.0089143 (Original work published 2014)

Chai, Q., Ferrell, B., Zhong, M., Zhang, X., Ye, C., & Wei, Y. (2014). Diverse sequences are functional at the C-terminus of the E. coli periplasmic chaperone SurA. Protein Engineering, Design & Selection : PEDS, 27(4), 111-6. https://doi.org/10.1093/protein/gzu003

Ye, C., Wang, Z., Lu, W., & Wei, Y. (2014). Unfolding study of a trimeric membrane protein AcrB. Protein Science : A Publication of the Protein Society, 23(7), 897-905. https://doi.org/10.1002/pro.2471

Ye, C., Wang, Z., Lu, W., Zhong, M., Chai, Q., & Wei, Y. (2014). Correlation between AcrB trimer association affinity and efflux activity. Biochemistry, 53(23), 3738-46. https://doi.org/10.1021/bi5000838 (Original work published 2014)

Gajadeera, C., Zhang, X., Wei, Y., & Tsodikov, O. (2015). Structure of inorganic pyrophosphatase from Staphylococcus aureus reveals conformational flexibility of the active site. Journal of Structural Biology, 189(2), 81-6. https://doi.org/10.1016/j.jsb.2014.12.003