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K
Kobe, M. J., Neau, D. B., Mitchell, C. E., Bartlett, S. G., and Newcomer, M. E. (2014) The structure of human 15-lipoxygenase-2 with a substrate mimic. J Biol Chem. 289, 8562-9
Koirala, D., Lewicka, A., Koldobskaya, Y., Huang, H., and Piccirilli, J. A. (2019) Synthetic Antibody Binding to a Preorganized RNA Domain of Hepatitis C Virus Internal Ribosome Entry Site Inhibits Translation. ACS Chem Biol. 10.1021/acschembio.9b00785
Köksal, M., Hu, H., Coates, R. M., Peters, R. J., and Christianson, D. W. (2011) Structure and mechanism of the diterpene cyclase ent-copalyl diphosphate synthase. Nat Chem Biol. 7, 431-3
Kono, A., Chou, T. - H., Radhakrishnan, A., Bolla, J. Reddy, Sankar, K., Shome, S., Su, C. - C., Jernigan, R. L., Robinson, C. V., Yu, E. W., and Spalding, M. H. (2020) Structure and Function of LCI1: A plasma membrane CO channel in the Chlamydomonas CO concentrating mechanism. Plant J. 10.1111/tpj.14745
Korasick, D. A., Končitíková, R., Kopečná, M., Hájková, E., Vigouroux, A., Moréra, S., Becker, D. F., Šebela, M., Tanner, J. J., and Kopečný, D. (2019) Structural and Biochemical Characterization of Aldehyde Dehydrogenase 12, the Last Enzyme of Proline Catabolism in Plants. J Mol Biol. 431, 576-592
Korasick, D. A., Owuocha, L. F., Kandoth, P. K., Tanner, J. J., Mitchum, M. G., and Beamer, L. J. (2023) Structural and functional analysis of two SHMT8 variants associated with soybean cyst nematode resistance. FEBS J. 10.1111/febs.16971
Kozlov, G., Mattijssen, S., Jiang, J., Nyandwi, S., Sprules, T., Iben, J. R., Coon, S. L., Gaidamakov, S., Noronha, A. M., Wilds, C. J., Maraia, R. J., and Gehring, K. (2022) Structural basis of 3'-end poly(A) RNA recognition by LARP1. Nucleic Acids Res. 10.1093/nar/gkac696
Krishnan, V., Dwivedi, P., Kim, B. J., Samal, A., Macon, K., Ma, X., Mishra, A., Doran, K. S., Ton-That, H., and Narayana, S. V. L. (2013) Structure of Streptococcus agalactiae tip pilin GBS104: a model for GBS pili assembly and host interactions. Acta Crystallogr D Biol Crystallogr. 69, 1073-89
Krochmal, D., Shao, Y., Li, N. - S., DasGupta, S., Shelke, S. A., Koirala, D., and Piccirilli, J. A. (2022) Structural basis for substrate binding and catalysis by a self-alkylating ribozyme. Nat Chem Biol. 10.1038/s41589-021-00950-z
Krochmal, D., Roman, C., Lewicka, A., Shao, Y., and Piccirilli, J. A. (2024) Structural basis for promiscuity in ligand recognition by yjdF riboswitch. Cell Discov. 10, 37
Kruidenier, L., Chung, C. -wa, Cheng, Z., Liddle, J., Che, K. H., Joberty, G., Bantscheff, M., Bountra, C., Bridges, A., Diallo, H., Eberhard, D., Hutchinson, S., Jones, E., Katso, R., Leveridge, M., Mander, P. K., Mosley, J., Ramirez-Molina, C., Rowland, P., Schofield, C. J., Sheppard, R. J., Smith, J. E., Swales, C., Tanner, R., Thomas, P., Tumber, A., Drewes, G., Oppermann, U., Patel, D. J., Lee, K., and Wilson, D. M. (2012) A selective jumonji H3K27 demethylase inhibitor modulates the proinflammatory macrophage response. Nature. 488, 404-8
Kucera, K., A Koblansky, A., Saunders, L. P., Frederick, K. B., De La Cruz, E. M., Ghosh, S., and Modis, Y. (2010) Structure-based analysis of Toxoplasma gondii profilin: a parasite-specific motif is required for recognition by Toll-like receptor 11. J Mol Biol. 403, 616-29
Kudalkar, S. N., Beloor, J., Chan, A. H., Lee, W. - G., Jorgensen, W. L., Kumar, P., and Anderson, K. S. (2017) Structural and Preclinical Studies of Computationally Designed Non-Nucleoside Reverse Transcriptase Inhibitors for Treating HIV infection. Mol Pharmacol. 91, 383-391
Kudalkar, S. N., Ullah, I., Bertoletti, N., Mandl, H. K., Cisneros, J. A., Beloor, J., Chan, A. H., Quijano, E., W Saltzman, M., Jorgensen, W. L., Kumar, P., and Anderson, K. S. (2019) Structural and pharmacological evaluation of a novel non-nucleoside reverse transcriptase inhibitor as a promising long acting nanoformulation for treating HIV. Antiviral Res. 167, 110-116
Kumar, S., Krishnamoorthy, K., Mudeppa, D. G., and Rathod, P. K. (2015) Structure of Plasmodium falciparum orotate phosphoribosyltransferase with autologous inhibitory protein-protein interactions. Acta Crystallogr F Struct Biol Commun. 71, 600-8
Kumar, S., Athreya, A., Gulati, A., Nair, R. Mony, Mahendran, I., Ranjan, R., and Penmatsa, A. (2021) Structural basis of inhibition of a transporter from Staphylococcus aureus, NorC, through a single-domain camelid antibody. Commun Biol. 4, 836
Kumar, S., Zavaliev, R., Wu, Q., Zhou, Y., Cheng, J., Dillard, L., Powers, J., Withers, J., Zhao, J., Guan, Z., Borgnia, M. J., Bartesaghi, A., Dong, X., and Zhou, P. (2022) Structural basis of NPR1 in activating plant immunity. Nature. 605, 561-566
Kuzina, E. S., Ung, P. Man- Un, Mohanty, J., Tome, F., Choi, J., Pardon, E., Steyaert, J., Lax, I., Schlessinger, A., Schlessinger, J., and Lee, S. (2019) Structures of ligand-occupied β-Klotho complexes reveal a molecular mechanism underlying endocrine FGF specificity and activity.. Proc Natl Acad Sci U S A. 116, 7819-7824
Kwak, S. - H., C Cochrane, S., Ennis, A. F., Lim, W. Young, Webster, C. G., Cho, J., Fenton, B. A., Zhou, P., and Hong, J. (2020) Synthesis and evaluation of sulfonyl piperazine LpxH inhibitors. Bioorg Chem. 102, 104055
Kwon, Y., Kaake, R. M., Echeverria, I., Suarez, M., Shamsabadi, M. Karimian, Stoneham, C., Ramirez, P. W., Kress, J., Singh, R., Sali, A., Krogan, N., Guatelli, J., and Jia, X. (2020) Structural basis of CD4 downregulation by HIV-1 Nef. Nat Struct Mol Biol. 10.1038/s41594-020-0463-z
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Lai, Y. - T., Tsai, K. - L., Sawaya, M. R., Asturias, F. J., and Yeates, T. O. (2013) Structure and flexibility of nanoscale protein cages designed by symmetric self-assembly. J Am Chem Soc. 135, 7738-43
Lai, Y. - T., Reading, E., Hura, G. L., Tsai, K. - L., Laganowsky, A., Asturias, F. J., Tainer, J. A., Robinson, C. V., and Yeates, T. O. (2014) Structure of a designed protein cage that self-assembles into a highly porous cube. Nat Chem. 6, 1065-71
Lai, Y. - T., Cascio, D., and Yeates, T. O. (2012) Structure of a 16-nm cage designed by using protein oligomers. Science. 336, 1129
Lai, M. - Y., Zhang, D., LaRonde-LeBlanc, N., and Fushman, D. (2012) Structural and biochemical studies of the open state of Lys48-linked diubiquitin. Biochim Biophys Acta. 1823, 2046-56
Laing, E. D., Navaratnarajah, C. K., Da Silva, S. Cheliout, Petzing, S. R., Xu, Y., Sterling, S. L., Marsh, G. A., Wang, L. - F., Amaya, M., Nikolov, D. B., Cattaneo, R., Broder, C. C., and Xu, K. (2019) Structural and functional analyses reveal promiscuous and species specific use of ephrin receptors by Cedar virus. Proc Natl Acad Sci U S A. 116, 20707-20715

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