Publications

Found 1282 results
Filters: First Letter Of Last Name is K  [Clear All Filters]
A B C D E F G H I J K L M N O P Q R S T U V W X Y Z 
T
Lepore, R., Kryshtafovych, A., Alahuhta, M., Veraszto, H. A., Bomble, Y. J., Bufton, J. C., Bullock, A. N., Caba, C., Cao, H., Davies, O. R., Desfosses, A., Dunne, M., Fidelis, K., Goulding, C. W., Gurusaran, M., Gutsche, I., Harding, C. J., Hartmann, M. D., Hayes, C. S., Joachimiak, A., Leiman, P. G., Loppnau, P., Lovering, A. L., Lunin, V. V., Michalska, K., Mir-Sanchis, I., Mitra, A. K., Moult, J., Phillips, G. N., Pinkas, D. M., Rice, P. A., Tong, Y., Topf, M., Walton, J. D., and Schwede, T. (2019) Target highlights in CASP13: Experimental target structures through the eyes of their authors. Proteins. 87, 1037-1057
Stafford, R. L., Hinde, E., Knight, M. Jane, Pennella, M. A., Ear, J., Digman, M. A., Gratton, E., and Bowie, J. U. (2011) Tandem SAM domain structure of human Caskin1: a presynaptic, self-assembling scaffold for CASK. Structure. 19, 1826-36
McMillan, B. J., Schnute, B., Ohlenhard, N., Zimmerman, B., Miles, L., Beglova, N., Klein, T., and Blacklow, S. C. (2015) A tail of two sites: a bipartite mechanism for recognition of notch ligands by mind bomb E3 ligases. Mol Cell. 57, 912-924
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
S
Zhang, W., Wu, K. - P., Sartori, M. A., Kamadurai, H. B., Ordureau, A., Jiang, C., Mercredi, P. Y., Murchie, R., Hu, J., Persaud, A., Mukherjee, M., Li, N., Doye, A., Walker, J. R., Sheng, Y., Hao, Z., Li, Y., Brown, K. R., Lemichez, E., Chen, J., Tong, Y., J Harper, W., Moffat, J., Rotin, D., Schulman, B. A., and Sidhu, S. S. (2016) System-Wide Modulation of HECT E3 Ligases with Selective Ubiquitin Variant Probes. Mol Cell. 62, 121-36
G Forse, J., Ram, N., D Banatao, R., Cascio, D., Sawaya, M. R., Klock, H. E., Lesley, S. A., and Yeates, T. O. (2011) Synthetic symmetrization in the crystallization and structure determination of CelA from Thermotoga maritima. Protein Sci. 20, 168-78
Reinke, A. W., Grant, R. A., and Keating, A. E. (2010) A synthetic coiled-coil interactome provides heterospecific modules for molecular engineering. J Am Chem Soc. 132, 6025-31
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
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
Mukherjee, S., Erramilli, S. K., Ammirati, M., Alvarez, F. J. D., Fennell, K. F., Purdy, M. D., Skrobek, B. M., Radziwon, K., Coukos, J., Kang, Y., Dutka, P., Gao, X., Qiu, X., Yeager, M., H Xu, E., Han, S., and Kossiakoff, A. A. (2020) Synthetic antibodies against BRIL as universal fiducial marks for single-particle cryoEM structure determination of membrane proteins. Nat Commun. 11, 1598
Mukherjee, S., Erramilli, S. K., Ammirati, M., Alvarez, F. J. D., Fennell, K. F., Purdy, M. D., Skrobek, B. M., Radziwon, K., Coukos, J., Kang, Y., Dutka, P., Gao, X., Qiu, X., Yeager, M., H Xu, E., Han, S., and Kossiakoff, A. A. (2020) Synthetic antibodies against BRIL as universal fiducial marks for single-particle cryoEM structure determination of membrane proteins. Nat Commun. 11, 1598
Mitcheltree, M. J., Pisipati, A., Syroegin, E. A., Silvestre, K. J., Klepacki, D., Mason, J. D., Terwilliger, D. W., Testolin, G., Pote, A. R., J Y Wu, K., Ladley, R. Porter, Chatman, K., Mankin, A. S., Polikanov, Y. S., and Myers, A. G. (2021) A synthetic antibiotic class overcoming bacterial multidrug resistance. Nature. 10.1038/s41586-021-04045-6
Nakaya, T., Yabe, M., Mashalidis, E. H., Sato, T., Yamamoto, K., Hikiji, Y., Katsuyama, A., Shinohara, M., Minato, Y., Takahashi, S., Horiuchi, M., Yokota, S. - I., Lee, S. - Y., and Ichikawa, S. (2022) Synthesis of macrocyclic nucleoside antibacterials and their interactions with MraY. Nat Commun. 13, 7575
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
Zheng, Y., Qiu, Y., Grace, C. R. R., Liu, X., Klionsky, D. J., and Schulman, B. A. (2019) A switch element in the autophagy E2 Atg3 mediates allosteric regulation across the lipidation cascade. Nat Commun. 10, 3600
Dubiella, C., Pinch, B. J., Koikawa, K., Zaidman, D., Poon, E., Manz, T. D., Nabet, B., He, S., Resnick, E., Rogel, A., Langer, E. M., Daniel, C. J., Seo, H. - S., Chen, Y., Adelmant, G., Sharifzadeh, S., Ficarro, S. B., Jamin, Y., da Costa, B. Martins, Zimmerman, M. W., Lian, X., Kibe, S., Kozono, S., Doctor, Z. M., Browne, C. M., Yang, A., Stoler-Barak, L., Shah, R. B., Vangos, N. E., Geffken, E. A., Oren, R., Koide, E., Sidi, S., Shulman, Z., Wang, C., Marto, J. A., Dhe-Paganon, S., Look, T., Zhou, X. Zhen, Lu, K. Ping, Sears, R. C., Chesler, L., Gray, N. S., and London, N. (2021) Sulfopin is a covalent inhibitor of Pin1 that blocks Myc-driven tumors in vivo. Nat Chem Biol. 10.1038/s41589-021-00786-7
Dubiella, C., Pinch, B. J., Koikawa, K., Zaidman, D., Poon, E., Manz, T. D., Nabet, B., He, S., Resnick, E., Rogel, A., Langer, E. M., Daniel, C. J., Seo, H. - S., Chen, Y., Adelmant, G., Sharifzadeh, S., Ficarro, S. B., Jamin, Y., da Costa, B. Martins, Zimmerman, M. W., Lian, X., Kibe, S., Kozono, S., Doctor, Z. M., Browne, C. M., Yang, A., Stoler-Barak, L., Shah, R. B., Vangos, N. E., Geffken, E. A., Oren, R., Koide, E., Sidi, S., Shulman, Z., Wang, C., Marto, J. A., Dhe-Paganon, S., Look, T., Zhou, X. Zhen, Lu, K. Ping, Sears, R. C., Chesler, L., Gray, N. S., and London, N. (2021) Sulfopin is a covalent inhibitor of Pin1 that blocks Myc-driven tumors in vivo. Nat Chem Biol. 10.1038/s41589-021-00786-7
Dubiella, C., Pinch, B. J., Koikawa, K., Zaidman, D., Poon, E., Manz, T. D., Nabet, B., He, S., Resnick, E., Rogel, A., Langer, E. M., Daniel, C. J., Seo, H. - S., Chen, Y., Adelmant, G., Sharifzadeh, S., Ficarro, S. B., Jamin, Y., da Costa, B. Martins, Zimmerman, M. W., Lian, X., Kibe, S., Kozono, S., Doctor, Z. M., Browne, C. M., Yang, A., Stoler-Barak, L., Shah, R. B., Vangos, N. E., Geffken, E. A., Oren, R., Koide, E., Sidi, S., Shulman, Z., Wang, C., Marto, J. A., Dhe-Paganon, S., Look, T., Zhou, X. Zhen, Lu, K. Ping, Sears, R. C., Chesler, L., Gray, N. S., and London, N. (2021) Sulfopin is a covalent inhibitor of Pin1 that blocks Myc-driven tumors in vivo. Nat Chem Biol. 10.1038/s41589-021-00786-7
Dubiella, C., Pinch, B. J., Koikawa, K., Zaidman, D., Poon, E., Manz, T. D., Nabet, B., He, S., Resnick, E., Rogel, A., Langer, E. M., Daniel, C. J., Seo, H. - S., Chen, Y., Adelmant, G., Sharifzadeh, S., Ficarro, S. B., Jamin, Y., da Costa, B. Martins, Zimmerman, M. W., Lian, X., Kibe, S., Kozono, S., Doctor, Z. M., Browne, C. M., Yang, A., Stoler-Barak, L., Shah, R. B., Vangos, N. E., Geffken, E. A., Oren, R., Koide, E., Sidi, S., Shulman, Z., Wang, C., Marto, J. A., Dhe-Paganon, S., Look, T., Zhou, X. Zhen, Lu, K. Ping, Sears, R. C., Chesler, L., Gray, N. S., and London, N. (2021) Sulfopin is a covalent inhibitor of Pin1 that blocks Myc-driven tumors in vivo. Nat Chem Biol. 10.1038/s41589-021-00786-7
Windsor, M. A., Hermanson, D. J., Kingsley, P. J., Xu, S., Crews, B. C., Ho, W., Keenan, C. M., Banerjee, S., Sharkey, K. A., and Marnett, L. J. (2012) Substrate-Selective Inhibition of Cyclooxygenase-2: Development and Evaluation of Achiral Profen Probes. ACS Med Chem Lett. 3, 759-763
Windsor, M. A., Hermanson, D. J., Kingsley, P. J., Xu, S., Crews, B. C., Ho, W., Keenan, C. M., Banerjee, S., Sharkey, K. A., and Marnett, L. J. (2012) Substrate-Selective Inhibition of Cyclooxygenase-2: Development and Evaluation of Achiral Profen Probes. ACS Med Chem Lett. 3, 759-763
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
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
Taabazuing, C. Y., Fermann, J., Garman, S., and Knapp, M. J. (2016) Substrate Promotes Productive Gas Binding in the α-Ketoglutarate-Dependent Oxygenase FIH.. Biochemistry. 55, 277-86
Schaefer, K., Owens, T. W., Kahne, D., and Walker, S. (2018) Substrate Preferences Establish the Order of Cell Wall Assembly in Staphylococcus aureus. J Am Chem Soc. 140, 2442-2445

Pages