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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
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
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
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
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
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
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
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, 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
Kim, C. Y., Mitchell, A. J., Kastner, D. W., Albright, C. E., Gutierrez, M. A., Glinkerman, C. M., Kulik, H. J., and Weng, J. - K. (2023) Emergence of a proton exchange-based isomerization and lactonization mechanism in the plant coumarin synthase COSY. Nat Commun. 14, 597
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, 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, 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, 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
Kimani, S. W., Owen, J., Green, S. R., Li, F., Li, Y., Dong, A., Brown, P. J., Ackloo, S., Kuter, D., Yang, C., MacAskill, M., MacKinnon, S. Scott, Arrowsmith, C. H., Schapira, M., Shahani, V., and Halabelian, L. (2023) Discovery of a Novel DCAF1 Ligand Using a Drug-Target Interaction Prediction Model: Generalizing Machine Learning to New Drug Targets. J Chem Inf Model. 63, 4070-4078
Kimani, S. W., Perveen, S., Szewezyk, M., Zeng, H., Dong, A., Li, F., Ghiabi, P., Li, Y., Chau, I., Arrowsmith, C. H., Barsyte-Lovejoy, D., Santhakumar, V., Vedadi, M., and Halabelian, L. (2023) The co-crystal structure of Cbl-b and a small-molecule inhibitor reveals the mechanism of Cbl-b inhibition. Commun Biol. 6, 1272
King, N. P., Jacobitz, A. W., Sawaya, M. R., Goldschmidt, L., and Yeates, T. O. (2010) Structure and folding of a designed knotted protein. Proc Natl Acad Sci U S A. 107, 20732-7
King, N. P., Bale, J. B., Sheffler, W., McNamara, D. E., Gonen, S., Gonen, T., Yeates, T. O., and Baker, D. (2014) Accurate design of co-assembling multi-component protein nanomaterials. Nature. 510, 103-8
King, N. P., Sheffler, W., Sawaya, M. R., Vollmar, B. S., Sumida, J. P., André, I., Gonen, T., Yeates, T. O., and Baker, D. (2012) Computational design of self-assembling protein nanomaterials with atomic level accuracy. Science. 336, 1171-4
Kirouac, K. N., and Ling, H. (2009) Structural basis of error-prone replication and stalling at a thymine base by human DNA polymerase iota. EMBO J. 28, 1644-54
Kirouac, K. N., and Ling, H. (2011) Unique active site promotes error-free replication opposite an 8-oxo-guanine lesion by human DNA polymerase iota. Proc Natl Acad Sci U S A. 108, 3210-5
Kirouac, K. N., Basu, A. K., and Ling, H. (2013) Structural mechanism of replication stalling on a bulky amino-polycyclic aromatic hydrocarbon DNA adduct by a y family DNA polymerase. J Mol Biol. 425, 4167-76

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