Wang, X., Zong, Y., Zhou, X., Xu, L., He, W., and Quan, S. Artificial Intelligence-Powered Construction of a Microbial Optimal Growth Temperature Database and Its Impact on Enzyme Optimal Temperature Prediction. J Phys Chem B (2024) 128(10): 2281-2292.

He, W., Yang, Y., Qian, Y., Chen, Z., Zheng, Y., Zhao, W., Yan, C., Guo, Z., and Quan, S. Fluorogenic sensing of amorphous aggregates, amyloid fibers, and chaperone activity via a near-infrared aggregation-induced emission-active probe. Aggregate (2024) 5(1): e412.

Xue, Z. X., and Quan, S. Understanding the Stabilization Mechanism of a Thermostable Mutant of Hygromycin B Phosphotransferase by Protein Sector-Guided Dynamic Analysis. Acs Omega (2023) 8(29): 25739-25748.

Li, Y., Zhao, L., Zhang, Y., Wu, P., Xu, Y., Mencius, J., Zheng, Y., Wang, X., Xu, W., Huang, N., Ye, X., Lei, M., Shi, P., Tian, C., Peng, C., Li, G., Liu, Z., Quan, S., and Chen, Y. Structural basis for product specificities of MLL family methyltransferases. Mol Cell (2022) 82(20): 3810-3825.

He, W., Li, X. M., Xue, H. J., Yang, Y. Y., Mencius, J., Bai, L., Zhang, J. Y., Xu, J. H., Wu, B., Xue, Y., and Quan, S. Insights into the client protein release mechanism of the ATP-independent chaperone Spy. Nat Commun (2022) 13(1): 2818.

Ren, C., Zheng, Y., Liu, C., Mencius, J., Wu, Z., and Quan, S. Molecular Characterization of an Intrinsically Disordered Chaperone Reveals Net-Charge Regulation in Chaperone Action. J Mol Biol (2022) 434(5): 167405.

He, W., Yu, G., Li, T., Bai, L., Yang, Y., Xue, Z., Pang, Y., Reichmann, D., Hiller, S., He, L., Liu, M., and Quan, S. Chaperone Spy Protects Outer Membrane Proteins from Folding Stress via Dynamic Complex Formation. mBio (2021) 12(5): e0213021.

Ren, C., Wen, X., Mencius, J., and Quan, S. An enzyme-based biosensor for monitoring and engineering protein stability in vivo. Proc Natl Acad Sci U S A (2021) 118(13): e2101618118.

Zheng, Y., Huang, Y., Mencius, J., Li, Y., Zhao, L., Luo, W., Chen, Y., and Quan, S. Distinct kinetic mechanisms of H3K4 methylation catalyzed by MLL3 and MLL4 core complexes. J Biol Chem (2021) 296: 100635.

He, W., Zhang, J., Sachsenhauser, V., Wang, L., Bardwell, J. C. A., and Quan, S. Increased surface charge in the protein chaperone Spy enhances its anti-aggregation activity. J Biol Chem (2020) 295(42): 14488-14500.