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Kim, K. - H., Ko, D. - K., Kim, Y. - T., Kim, N. Hyeong, Paul, J., Zhang, S. - Q., Murray, C. B., Acharya, R., DeGrado, W. F., Kim, Y. Ho, and Grigoryan, G. (2016) Protein-directed self-assembly of a fullerene crystal. Nat Commun. 7, 11429
Kim, S. - A., Zhu, J., Yennawar, N., Eek, P., and Tan, S. (2020) Crystal Structure of the LSD1/CoREST Histone Demethylase Bound to Its Nucleosome Substrate. Mol Cell. 10.1016/j.molcel.2020.04.019
Kim, S., Grant, R. A., and Sauer, R. T. (2011) Covalent linkage of distinct substrate degrons controls assembly and disassembly of DegP proteolytic cages. Cell. 145, 67-78
Kim, S. Kyung, Barron, L., Hinck, C. S., Petrunak, E. M., Cano, K. E., Thangirala, A., Iskra, B., Brothers, M., Vonberg, M., Leal, B., Richter, B., Kodali, R., Taylor, A. B., Du, S., Barnes, C. O., Sulea, T., Calero, G., P Hart, J., Hart, M. J., Demeler, B., and Hinck, A. P. (2017) An engineered transforming growth factor β (TGF-β) monomer that functions as a dominant negative to block TGF-β signaling.. J Biol Chem. 292, 7173-7188
Kim, Y., Rosenberg, S. C., Kugel, C. L., Kostow, N., Rog, O., Davydov, V., Su, T. Y., Dernburg, A. F., and Corbett, K. D. (2014) The chromosome axis controls meiotic events through a hierarchical assembly of HORMA domain proteins. Dev Cell. 31, 487-502
Kim, D. E., Jensen, D. R., Feldman, D., Tischer, D., Saleem, A., Chow, C. M., Li, X., Carter, L., Milles, L., Nguyen, H., Kang, A., Bera, A. K., Peterson, F. C., Volkman, B. F., Ovchinnikov, S., and Baker, D. (2023) De novo design of small beta barrel proteins. Proc Natl Acad Sci U S A. 120, e2207974120
Kim, M., Sandford, E., Gatica, D., Qiu, Y., Liu, X., Zheng, Y., Schulman, B. A., Xu, J., Semple, I., Ro, S. - H., Kim, B., R Mavioglu, N., Tolun, A., Jipa, A., Takats, S., Karpati, M., Li, J. Z., Yapici, Z., Juhasz, G., Lee, J. Hee, Klionsky, D. J., and Burmeister, M. (2016) Mutation in ATG5 reduces autophagy and leads to ataxia with developmental delay. Elife. 10.7554/eLife.12245
Kiburu, I. N., and LaRonde-LeBlanc, N. (2012) Interaction of Rio1 kinase with toyocamycin reveals a conformational switch that controls oligomeric state and catalytic activity. PLoS One. 7, e37371
Khare, B., Samal, A., Vengadesan, K., Rajashankar, K. R., Ma, X., I Huang, H., Ton-That, H., and Narayana, S. V. L. (2010) Preliminary crystallographic study of the Streptococcus agalactiae sortases, sortase A and sortase C1. Acta Crystallogr Sect F Struct Biol Cryst Commun. 66, 1096-100
Khare, B., Krishnan, V., Rajashankar, K. R., I-Hsiu, H., Xin, M., Ton-That, H., and Narayana, S. V. (2011) Structural differences between the Streptococcus agalactiae housekeeping and pilus-specific sortases: SrtA and SrtC1. PLoS One. 6, e22995
Khan, N., Pelletier, D., McAlear, T. S., Croteau, N., Veyron, S., Bayne, A. N., Black, C., Ichikawa, M., Khalifa, A. Abdelzaher, Chaaban, S., Kurinov, I., Brouhard, G., Bechstedt, S., Bui, K. Huy, and Trempe, J. - F. (2021) Crystal structure of human PACRG in complex with MEIG1 reveals roles in axoneme formation and tubulin binding. Structure. 29, 572-586.e6
Khadka, N., Farquhar, E. R., Hill, H. E., Shi, W., von Lintig, J., and Kiser, P. D. (2019) Evidence for distinct rate-limiting steps in the cleavage of alkenes by carotenoid cleavage dioxygenases. J Biol Chem. 10.1074/jbc.RA119.007535
Khabibullina, N. F., Tereshchenkov, A. G., Komarova, E. S., Syroegin, E. A., Shiriaev, D. I., Paleskava, A., Kartsev, V. G., Bogdanov, A. A., Konevega, A. L., Dontsova, O. A., Sergiev, P. V., Osterman, I. A., and Polikanov, Y. S. (2019) Structure of dirithromycin bound to the bacterial ribosome suggests new ways for rational improvement of macrolides. Antimicrob Agents Chemother. 10.1128/AAC.02266-18
Ketkar, A., Zafar, M. K., Banerjee, S., Marquez, V. E., Egli, M., and Eoff, R. L. (2012) Differential furanose selection in the active sites of archaeal DNA polymerases probed by fixed-conformation nucleotide analogues. Biochemistry. 51, 9234-44
Ketkar, A., Zafar, M. K., Banerjee, S., Marquez, V. E., Egli, M., and Eoff, R. L. (2012) A nucleotide-analogue-induced gain of function corrects the error-prone nature of human DNA polymerase iota. J Am Chem Soc. 134, 10698-705
Ketkar, A., Zafar, M. K., Maddukuri, L., Yamanaka, K., Banerjee, S., Egli, M., Choi, J. - Y., R Lloyd, S., and Eoff, R. L. (2013) Leukotriene biosynthesis inhibitor MK886 impedes DNA polymerase activity. Chem Res Toxicol. 26, 221-32
Ketcham, J. M., Harwood, S. J., Aranda, R., Aloiau, A. N., Bobek, B. M., Briere, D. M., Burns, A. C., Haatveit, K. Caddell, Calinisan, A., Clarine, J., Elliott, A., Engstrom, L. D., Gunn, R. J., Ivetac, A., Jones, B., Kuehler, J., J Lawson, D., Nguyen, N., Parker, C., Pearson, K. E., Rahbaek, L., Saechao, B., Wang, X., Waters, A., Waters, L., Watkins, A. H., Olson, P., Smith, C. R., Christensen, J. G., and Marx, M. A. (2024) Discovery of Pyridopyrimidinones that Selectively Inhibit the H1047R PI3Kα Mutant Protein.. J Med Chem. 67, 4936-4949
Ketcham, J. M., Haling, J., Khare, S., Bowcut, V., Briere, D. M., Burns, A. C., Gunn, R. J., Ivetac, A., Kuehler, J., Kulyk, S., Laguer, J., J Lawson, D., Moya, K., Nguyen, N., Rahbaek, L., Saechao, B., Smith, C. R., Sudhakar, N., Thomas, N. C., Vegar, L., Vanderpool, D., Wang, X., Yan, L., Olson, P., Christensen, J. G., and Marx, M. A. (2022) Design and Discovery of MRTX0902, a Potent, Selective, Brain-Penetrant, and Orally Bioavailable Inhibitor of the SOS1:KRAS Protein-Protein Interaction. J Med Chem. 65, 9678-9690
Keszei, A. F. A., Tang, X., McCormick, C., Zeqiraj, E., Rohde, J. R., Tyers, M., and Sicheri, F. (2014) Structure of an SspH1-PKN1 complex reveals the basis for host substrate recognition and mechanism of activation for a bacterial E3 ubiquitin ligase. Mol Cell Biol. 34, 362-73
Kenoth, R., Simanshu, D. K., Kamlekar, R. Kanth, Pike, H. M., Molotkovsky, J. G., Benson, L. M., H Bergen, R., Prendergast, F. G., Malinina, L., Venyaminov, S. Y., Patel, D. J., and Brown, R. E. (2010) Structural determination and tryptophan fluorescence of heterokaryon incompatibility C2 protein (HET-C2), a fungal glycolipid transfer protein (GLTP), provide novel insights into glycolipid specificity and membrane interaction by the GLTP fold. J Biol Chem. 285, 13066-78
Kelso, S., O'Brien, S., Kurinov, I., Angers, S., and Sicheri, F. (2022) Crystal structure of the CDK11 kinase domain bound to the small-molecule inhibitor OTS964. Structure. 10.1016/j.str.2022.10.003
Kelso, S., Orlicky, S., Beenstock, J., Ceccarelli, D. F., Kurinov, I., Gish, G., and Sicheri, F. (2021) Bipartite binding of the N terminus of Skp2 to cyclin A. Structure. 10.1016/j.str.2021.04.011
Kelley, K., Knockenhauer, K. E., Kabachinski, G., and Schwartz, T. U. (2015) Atomic structure of the Y complex of the nuclear pore. Nat Struct Mol Biol. 22, 425-431
Keller, G. L. J., Weiss, L. I., and Baker, B. M. (2022) Physicochemical Heuristics for Identifying High Fidelity, Near-Native Structural Models of Peptide/MHC Complexes. Front Immunol. 13, 887759
Kearns, S. P., Swartz, P. D., Perry, K., Roy, T. A., D'Antonio, J., and D'Antonio, E. L. (2015) Exploration of Monosaccharide Inhibitors for Trypanosoma cruzi Glucokinase and Hexokinase. 66th Southeastern Regional Meeting of the American Chemical Society, October 16-19, 2015