Publications

Found 53 results
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Journal Article
Shaban, N. M., Shi, K., Li, M., Aihara, H., and Harris, R. S. (2016) 1.92 Angstrom Zinc-Free APOBEC3F Catalytic Domain Crystal Structure. J Mol Biol. 428, 2307-16
Cui, H., Carlson, A. S., Schleiff, M. A., Divakaran, A., Johnson, J. A., Buchholz, C. R., Zahid, H., Vail, N. R., Shi, K., Aihara, H., Harki, D. A., Miller, G. P., Topczewski, J. J., and Pomerantz, W. C. K. (2021) 4-Methyl-1,2,3-Triazoles as -Acetyl-Lysine Mimics Afford Potent BET Bromodomain Inhibitors with Improved Selectivity. J Med Chem. 64, 10497-10511
Shi, K., Demir, Ö., Carpenter, M. A., Banerjee, S., Harki, D. A., Amaro, R. E., Harris, R. S., and Aihara, H. (2020) Active site plasticity and possible modes of chemical inhibition of the human DNA deaminase APOBEC3B. FASEB Bioadv. 2, 49-58
Bosnakovski, D., Toso, E. A., Ener, E. T., Gearhart, M. D., Yin, L., Lüttmann, F. F., Magli, A., Shi, K., Kim, J., Aihara, H., and Kyba, M. (2023) Antagonism among DUX family members evolved from an ancestral toxic single homeodomain protein. iScience. 26, 107823
Shaban, N. M., Shi, K., Lauer, K. V., Carpenter, M. A., Richards, C. M., Salamango, D., Wang, J., Lopresti, M. W., Banerjee, S., Levin-Klein, R., Brown, W. L., Aihara, H., and Harris, R. S. (2018) The Antiviral and Cancer Genomic DNA Deaminase APOBEC3H Is Regulated by an RNA-Mediated Dimerization Mechanism. Mol Cell. 69, 75-86.e9
Shi, K., Demir, Ö., Carpenter, M. A., Wagner, J., Kurahashi, K., Harris, R. S., Amaro, R. E., and Aihara, H. (2017) Conformational Switch Regulates the DNA Cytosine Deaminase Activity of Human APOBEC3B. Sci Rep. 7, 17415
Shi, K., Kurniawan, F., Banerjee, S., Moeller, N. H., and Aihara, H. (2020) Crystal structure of bacteriophage T4 Spackle as determined by native SAD phasing. Acta Crystallogr D Struct Biol. 76, 899-904
Kurniawan, F., Shi, K., Kurahashi, K., Bielinsky, A. - K., and Aihara, H. (2018) Crystal Structure of Cdc45 Suggests a Conformational Switch that May Regulate DNA Replication. iScience. 3, 102-109
Bohl, T. E., Shi, K., Lee, J. K., and Aihara, H. (2018) Crystal structure of lipid A disaccharide synthase LpxB from Escherichia coli. Nat Commun. 9, 377
Shi, K., Carpenter, M. A., Kurahashi, K., Harris, R. S., and Aihara, H. (2015) Crystal Structure of the DNA Deaminase APOBEC3B Catalytic Domain. J Biol Chem. 290, 28120-30
Lee, J. K., Bosnakovski, D., Toso, E. A., Dinh, T., Banerjee, S., Bohl, T. E., Shi, K., Orellana, K., Kyba, M., and Aihara, H. (2018) Crystal Structure of the Double Homeodomain of DUX4 in Complex with DNA. Cell Rep. 25, 2955-2962.e3
Limón, L. K., Shi, K., Dao, A., Rugloski, J., Tompkins, K. J., Aihara, H., Gordon, W. R., and Evans, R. L. (2023) The crystal structure of the human smacovirus 1 Rep domain. Acta Crystallogr F Struct Biol Commun. 79, 295-300
Yin, Z., Shi, K., Banerjee, S., Pandey, K. K., Bera, S., Grandgenett, D. P., and Aihara, H. (2016) Crystal structure of the Rous sarcoma virus intasome. Nature. 530, 362-6
Everett, B. A., Litzau, L. A., Tompkins, K., Shi, K., Nelson, A., Aihara, H., Iii, R. L. Evans, and Gordon, W. R. (2019) Crystal structure of the Wheat dwarf virus Rep domain. Acta Crystallogr F Struct Biol Commun. 75, 744-749
Shi, K., Cho, S., Aukema, K. G., Lee, T., Bera, A. K., Seffernick, J. L., Wackett, L. P., and Aihara, H. (2019) Crystal structures of Moorella thermoacetica cyanuric acid hydrolase reveal conformational flexibility and asymmetry important for catalysis. PLoS One. 14, e0216979
Ye, G., Gallant, J., Zheng, J., Massey, C., Shi, K., Tai, W., Odle, A., Vickers, M., Shang, J., Wan, Y., Du, L., Aihara, H., Perlman, S., LeBeau, A., and Li, F. (2021) The development of Nanosota-1 as anti-SARS-CoV-2 nanobody drug candidates. Elife. 10.7554/eLife.64815
Klingler, C., Ashley, J., Shi, K., Stiefvater, A., Kyba, M., Sinnreich, M., Aihara, H., and Kinter, J. (2020) DNA aptamers against the DUX4 protein reveal novel therapeutic implications for FSHD. FASEB J. 34, 4573-4590
Tang, H., Shi, K., Shi, C., Aihara, H., Zhang, J., and Du, G. (2019) Enhancing subtilisin thermostability through a modified normalized B-factor analysis and loop-grafting strategy. J Biol Chem. 10.1074/jbc.RA119.010658
Shi, K., Huang, W. Mun, and Aihara, H. (2013) An enzyme-catalyzed multistep DNA refolding mechanism in hairpin telomere formation. PLoS Biol. 11, e1001472
Bertram, J. H., Mulliner, K. M., Shi, K., Plunkett, M. H., Nixon, P., Serratore, N. A., Douglas, C. J., Aihara, H., and Barney, B. M. (2017) Five Fatty Aldehyde Dehydrogenase Enzymes from Marinobacter and Acinetobacter spp. and Structural Insights into the Aldehyde Binding Pocket. Appl Environ Microbiol. 10.1128/AEM.00018-17
Moghadasi, S. Arad, Esler, M. A., Otsuka, Y., Becker, J. T., Moraes, S. N., Anderson, C. B., Chamakuri, S., Belica, C., Wick, C., Harki, D. A., Young, D. W., Scampavia, L., Spicer, T. P., Shi, K., Aihara, H., Brown, W. L., and Harris, R. S. (2022) Gain-of-Signal Assays for Probing Inhibition of SARS-CoV-2 M/3CL in Living Cells. mBio. 10.1128/mbio.00784-22
Talledge, N., Yang, H., Shi, K., Coray, R., Yu, G., Arndt, W. G., Meng, S., Baxter, G. C., Mendonça, L. M., Castaño-Díez, D., Aihara, H., Mansky, L. M., and Zhang, W. (2023) HIV-2 Immature Particle Morphology Provides Insights into Gag Lattice Stability and Virus Maturation. J Mol Biol. 10.1016/j.jmb.2023.168143
Tang, H., Zhang, J., Shi, K., Aihara, H., and Du, G. (2019) Insight into subtilisin E-S7 cleavage pattern based on crystal structure and hydrolysates peptide analysis. Biochem Biophys Res Commun. 10.1016/j.bbrc.2019.03.064
Huang, W. Mun, DaGloria, J., Fox, H., Ruan, Q., Tillou, J., Shi, K., Aihara, H., Aron, J., and Casjens, S. (2012) Linear chromosome-generating system of Agrobacterium tumefaciens C58: protelomerase generates and protects hairpin ends. J Biol Chem. 287, 25551-63
Ubah, O. C., Lake, E. W., Gunaratne, G. S., Gallant, J. P., Fernie, M., Robertson, A. J., Marchant, J. S., Bold, T. D., Langlois, R. A., Matchett, W. E., Thiede, J. M., Shi, K., Yin, L., Moeller, N. H., Banerjee, S., Ferguson, L., Kovaleva, M., Porter, A. J., Aihara, H., LeBeau, A. M., and Barelle, C. J. (2021) Mechanisms of SARS-CoV-2 neutralization by shark variable new antigen receptors elucidated through X-ray crystallography. Nat Commun. 12, 7325

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