Year |
Citation |
Score |
2021 |
He W, Yu G, Li T, Bai L, Yang Y, Xue Z, Pang Y, Reichmann D, Hiller S, He L, Liu M, Quan S. Chaperone Spy Protects Outer Membrane Proteins from Folding Stress via Dynamic Complex Formation. Mbio. e0213021. PMID 34607455 DOI: 10.1128/mBio.02130-21 |
0.357 |
|
2021 |
Ren C, Wen X, Mencius J, Quan S. 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. PMID 33753520 DOI: 10.1073/pnas.2101618118 |
0.388 |
|
2020 |
Chen G, Wang D, Wu B, Yan F, Xue H, Wang Q, Quan S, Chen Y. Taf14 recognizes a common motif in transcriptional machineries and facilitates their clustering by phase separation. Nature Communications. 11: 4206. PMID 32826896 DOI: 10.1038/S41467-020-18021-7 |
0.314 |
|
2020 |
He W, Zhang J, Sachsenhauser V, Wang L, Bardwell JCA, Quan S. Increased surface charge in the protein chaperone Spy enhances its anti-aggregation activity. The Journal of Biological Chemistry. PMID 32817055 DOI: 10.1074/Jbc.Ra119.012300 |
0.637 |
|
2019 |
Shang YP, Chen Q, Li AT, Quan S, Xu JH, Yu HL. Attenuated substrate inhibition of a haloketone reductase via structure-guided loop engineering. Journal of Biotechnology. PMID 31866427 DOI: 10.1016/J.Jbiotec.2019.12.011 |
0.307 |
|
2019 |
Ruan A, Ren C, Quan S. Conversion of the Molecular Chaperone Spy into a Novel Fusion Tag to Enhance Recombinant Protein Expression. Journal of Biotechnology. PMID 31705934 DOI: 10.1016/J.Jbiotec.2019.11.006 |
0.522 |
|
2019 |
Ren C, Wen X, Mencius J, Quan S. Selection and screening strategies in directed evolution to improve protein stability Bioresources and Bioprocessing. 6. DOI: 10.1186/S40643-019-0288-Y |
0.437 |
|
2018 |
Horowitz S, Salmon L, Koldewey P, Ahlstrom LS, Martin R, Quan S, Afonine PV, van den Bedem H, Wang L, Xu Q, Trievel RC, Brooks CL, Bardwell JCA. Reply to 'Misreading chaperone-substrate complexes from random noise'. Nature Structural & Molecular Biology. PMID 30297780 DOI: 10.1038/S41594-018-0145-2 |
0.525 |
|
2017 |
Bai L, He W, Li T, Yang C, Zhuang Y, Quan S. Chaperone-substrate interactions monitored via a robust TEM-1 β-lactamase fragment complementation assay. Biotechnology Letters. PMID 28492977 DOI: 10.1007/S10529-017-2347-9 |
0.491 |
|
2016 |
Horowitz S, Salmon L, Koldewey P, Ahlstrom LS, Martin R, Quan S, Afonine PV, van den Bedem H, Wang L, Xu Q, Trievel RC, Brooks CL, Bardwell JC. Visualizing chaperone-assisted protein folding. Nature Structural & Molecular Biology. PMID 27239796 DOI: 10.1038/Nsmb.3237 |
0.657 |
|
2014 |
Quan S, Wang L, Petrotchenko EV, Makepeace KA, Horowitz S, Yang J, Zhang Y, Borchers CH, Bardwell JC. Super Spy variants implicate flexibility in chaperone action. Elife. 3: e01584. PMID 24497545 DOI: 10.7554/Elife.01584 |
0.645 |
|
2013 |
Quan S, Hiniker A, Collet JF, Bardwell JC. Isolation of bacteria envelope proteins. Methods in Molecular Biology (Clifton, N.J.). 966: 359-66. PMID 23299746 DOI: 10.1007/978-1-62703-245-2_22 |
0.655 |
|
2012 |
Quan S, Bardwell JC. Chaperone discovery. Bioessays : News and Reviews in Molecular, Cellular and Developmental Biology. 34: 973-81. PMID 22968800 DOI: 10.1002/bies.201200059 |
0.658 |
|
2011 |
Evans ML, Schmidt JC, Ilbert M, Doyle SM, Quan S, Bardwell JC, Jakob U, Wickner S, Chapman MR. E. coli chaperones DnaK, Hsp33 and Spy inhibit bacterial functional amyloid assembly. Prion. 5: 323-34. PMID 22156728 DOI: 10.4161/Pri.18555 |
0.601 |
|
2011 |
Quan S, Koldewey P, Tapley T, Kirsch N, Ruane KM, Pfizenmaier J, Shi R, Hofmann S, Foit L, Ren G, Jakob U, Xu Z, Cygler M, Bardwell JC. Genetic selection designed to stabilize proteins uncovers a chaperone called Spy. Nature Structural & Molecular Biology. 18: 262-9. PMID 21317898 DOI: 10.1038/Nsmb.2016 |
0.683 |
|
2008 |
Masip L, Klein-Marcuschamer D, Quan S, Bardwell JC, Georgiou G. Laboratory evolution of Escherichia coli thioredoxin for enhanced catalysis of protein oxidation in the periplasm reveals a phylogenetically conserved substrate specificity determinant. The Journal of Biological Chemistry. 283: 840-8. PMID 18003618 DOI: 10.1074/Jbc.M705147200 |
0.596 |
|
2007 |
Quan S, Schneider I, Pan J, Von Hacht A, Bardwell JC. The CXXC motif is more than a redox rheostat. The Journal of Biological Chemistry. 282: 28823-33. PMID 17675287 DOI: 10.1074/Jbc.M705291200 |
0.653 |
|
2003 |
Chen Y, Lu YJ, Wang HW, Quan S, Chang Z, Sui SF. Two-dimensional crystallization of a small heat shock protein HSP16.3 on lipid layer. Biochemical and Biophysical Research Communications. 310: 360-6. PMID 14521918 DOI: 10.1016/J.Bbrc.2003.09.026 |
0.335 |
|
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