Publications

Found 58 results
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Xing, Q., Shi, K., Portaliou, A., Rossi, P., Economou, A., and Kalodimos, C. G. (2018) Structures of chaperone-substrate complexes docked onto the export gate in a type III secretion system. Nat Commun. 9, 1773
Chen, X., Randles, L., Shi, K., Tarasov, S. G., Aihara, H., and Walters, K. J. (2016) Structures of Rpn1 T1:Rad23 and hRpn13:hPLIC2 Reveal Distinct Binding Mechanisms between Substrate Receptors and Shuttle Factors of the Proteasome. Structure. 24, 1257-70
Bohl, T. E., Ieong, P., Lee, J. K., Lee, T., Kankanala, J., Shi, K., Demir, Ö., Kurahashi, K., Amaro, R. E., Wang, Z., and Aihara, H. (2018) The substrate-binding cap of the UDP-diacylglucosamine pyrophosphatase LpxH is highly flexible, enabling facile substrate binding and product release. J Biol Chem. 10.1074/jbc.RA118.002503
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Shi, K., Bohl, T. E., Park, J., Zasada, A., Malik, S., Banerjee, S., Tran, V., Li, N., Yin, Z., Kurniawan, F., Orellana, K., and Aihara, H. (2018) T4 DNA ligase structure reveals a prototypical ATP-dependent ligase with a unique mode of sliding clamp interaction. Nucleic Acids Res. 10.1093/nar/gky776
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Larson, G., Windsor, P., Smithwick, E., Shi, K., Aihara, H., Damodaran, A. Rama, and Bhagi-Damodaran, A. (2023) Understanding ATP binding to DosS catalytic domain with a short ATP-lid. bioRxiv. 10.1101/2023.05.29.542785
Larson, G. W., Windsor, P. K., Smithwick, E., Shi, K., Aihara, H., Damodaran, A. Rama, and Bhagi-Damodaran, A. (2023) Understanding ATP Binding to DosS Catalytic Domain with a Short ATP-Lid. Biochemistry. 62, 3283-3292
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Smiley, A. T., Tompkins, K. J., Pawlak, M. R., Krueger, A. J., Evans, R. L., Shi, K., Aihara, H., and Gordon, W. R. (2022) Watson-Crick Base-Pairing Requirements for ssDNA Recognition and Processing in Replication-Initiating HUH Endonucleases. mBio. 10.1128/mbio.02587-22
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Jones, J. C., Banerjee, R., Semonis, M. M., Shi, K., Aihara, H., and Lipscomb, J. D. (2022) X-ray Crystal Structures of Methane Monooxygenase Hydroxylase Complexes with Variants of Its Regulatory Component: Correlations with Altered Reaction Cycle Dynamics. Biochemistry. 61, 21-33

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