Shu Quan, Ph.D.

Affiliations: 
2010 University of Michigan, Ann Arbor, Ann Arbor, MI 
Area:
Microbiology Biology, Biochemistry, Genetics
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"Shu Quan"

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James Bardwell grad student 2010 University of Michigan
 (Directed evolution designed to optimize the in vivo protein folding environment.)
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Publications

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He W, Yu G, Li T, et al. (2021) Chaperone Spy Protects Outer Membrane Proteins from Folding Stress via Dynamic Complex Formation. Mbio. e0213021
Ren C, Wen X, Mencius J, et al. (2021) An enzyme-based biosensor for monitoring and engineering protein stability in vivo. Proceedings of the National Academy of Sciences of the United States of America. 118
Chen G, Wang D, Wu B, et al. (2020) Taf14 recognizes a common motif in transcriptional machineries and facilitates their clustering by phase separation. Nature Communications. 11: 4206
He W, Zhang J, Sachsenhauser V, et al. (2020) Increased surface charge in the protein chaperone Spy enhances its anti-aggregation activity. The Journal of Biological Chemistry
Shang YP, Chen Q, Li AT, et al. (2019) Attenuated substrate inhibition of a haloketone reductase via structure-guided loop engineering. Journal of Biotechnology
Ruan A, Ren C, Quan S. (2019) Conversion of the Molecular Chaperone Spy into a Novel Fusion Tag to Enhance Recombinant Protein Expression. Journal of Biotechnology
Ren C, Wen X, Mencius J, et al. (2019) Selection and screening strategies in directed evolution to improve protein stability Bioresources and Bioprocessing. 6
Horowitz S, Salmon L, Koldewey P, et al. (2018) Reply to 'Misreading chaperone-substrate complexes from random noise'. Nature Structural & Molecular Biology
Bai L, He W, Li T, et al. (2017) Chaperone-substrate interactions monitored via a robust TEM-1 β-lactamase fragment complementation assay. Biotechnology Letters
Horowitz S, Salmon L, Koldewey P, et al. (2016) Visualizing chaperone-assisted protein folding. Nature Structural & Molecular Biology
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