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Sankhala, R. S., Dussupt, V., Chen, W. - H., Bai, H., Martinez, E. J., Jensen, J. L., Rees, P. A., Hajduczki, A., Chang, W. C., Choe, M., Yan, L., Sterling, S. L., Swafford, I., Kuklis, C., Soman, S., King, J., Corbitt, C., Zemil, M., Peterson, C. E., Mendez-Rivera, L., Townsley, S. M., Donofrio, G. C., Lal, K. G., Tran, U., Green, E. C., Smith, C., de Val, N., Laing, E. D., Broder, C. C., Currier, J. R., Gromowski, G. D., Wieczorek, L., Rolland, M., Paquin-Proulx, D., van Dyk, D., Britton, Z., Rajan, S., Loo, Y. Ming, McTamney, P. M., Esser, M. T., Polonis, V. R., Michael, N. L., Krebs, S. J., Modjarrad, K., and M Joyce, G. (2023) Antibody targeting of conserved sites of vulnerability on the SARS-CoV-2 spike receptor-binding domain. Structure. 10.1016/j.str.2023.11.015
Tao, Y., Budhipramono, A., Huang, J., Fang, M., Xie, S., Kim, J., Khivansara, V., Dominski, Z., Tong, L., De Brabander, J. K., and Nijhawan, D. (2024) Anticancer benzoxaboroles block pre-mRNA processing by directly inhibiting CPSF3. Cell Chem Biol. 31, 139-149.e14
Tao, Y., Budhipramono, A., Huang, J., Fang, M., Xie, S., Kim, J., Khivansara, V., Dominski, Z., Tong, L., De Brabander, J. K., and Nijhawan, D. (2024) Anticancer benzoxaboroles block pre-mRNA processing by directly inhibiting CPSF3. Cell Chem Biol. 31, 139-149.e14
Bruce, H. A., Singer, A. U., Blazer, L. L., Luu, K., Ploder, L., Pavlenco, A., Kurinov, I., Adams, J. J., and Sidhu, S. S. (2024) Antigen-binding fragments with improved crystal lattice packing and enhanced conformational flexibility at the elbow region as crystallization chaperones. Protein Sci. 33, e5081
Uddin, M. Jashim, Crews, B. C., Xu, S., Ghebreselasie, K., Daniel, C. K., Kingsley, P. J., Banerjee, S., and Marnett, L. J. (2016) Antitumor Activity of Cytotoxic Cyclooxygenase-2 Inhibitors. ACS Chem Biol. 11, 3052-3060
Hanke, L., Knockenhauer, K. E., R Brewer, C., van Diest, E., Schmidt, F. I., Schwartz, T. U., and Ploegh, H. L. (2016) The Antiviral Mechanism of an Influenza A Virus Nucleoprotein-Specific Single-Domain Antibody Fragment. MBio. 10.1128/mBio.01569-16
Saxton, R. A., Knockenhauer, K. E., Schwartz, T. U., and Sabatini, D. M. (2016) The apo-structure of the leucine sensor Sestrin2 is still elusive. Sci Signal. 9, ra92
Moss, F. J., Mahinthichaichan, P., Lodowski, D. T., Kowatz, T., Tajkhorshid, E., Engel, A., Boron, W. F., and Vahedi-Faridi, A. (2020) Aquaporin-7: A Dynamic Aquaglyceroporin With Greater Water and Glycerol Permeability Than Its Bacterial Homolog GlpF. Front Physiol. 11, 728
Xie, W., Lama, L., Yang, X., Kuryavyi, V., Bhattacharya, S., Nudelman, I., Yang, G., Ouerfelli, O., J Glickman, F., Jones, R. A., Tuschl, T., and Patel, D. J. (2023) Arabinose- and xylose-modified analogs of 2',3'-cGAMP act as STING agonists. Cell Chem Biol. 10.1016/j.chembiol.2023.07.002
Park, E., Rawson, S., Li, K., Kim, B. - W., Ficarro, S. B., Del Pino, G. Gonzalez-, Sharif, H., Marto, J. A., Jeon, H., and Eck, M. J. (2019) Architecture of autoinhibited and active BRAF-MEK1-14-3-3 complexes. Nature. 575, 545-550
Dayeh, D. M., Cantara, W. A., Kitzrow, J. P., Musier-Forsyth, K., and Nakanishi, K. (2018) Argonaute-based programmable RNase as a tool for cleavage of highly-structured RNA. Nucleic Acids Res. 46, e98
Kozono, S., Lin, Y. - M., Seo, H. - S., Pinch, B., Lian, X., Qiu, C., Herbert, M. K., Chen, C. - H., Tan, L., Gao, Z. Jeff, Massefski, W., Doctor, Z. M., Jackson, B. P., Chen, Y., Dhe-Paganon, S., Lu, K. Ping, and Zhou, X. Zhen (2018) Arsenic targets Pin1 and cooperates with retinoic acid to inhibit cancer-driving pathways and tumor-initiating cells. Nat Commun. 9, 3069
Taherbhoy, A. M., Tait, S. W., Kaiser, S. E., Williams, A. H., Deng, A., Nourse, A., Hammel, M., Kurinov, I., Rock, C. O., Green, D. R., and Schulman, B. A. (2011) Atg8 transfer from Atg7 to Atg3: a distinctive E1-E2 architecture and mechanism in the autophagy pathway. Mol Cell. 44, 451-61
Taherbhoy, A. M., Tait, S. W., Kaiser, S. E., Williams, A. H., Deng, A., Nourse, A., Hammel, M., Kurinov, I., Rock, C. O., Green, D. R., and Schulman, B. A. (2011) Atg8 transfer from Atg7 to Atg3: a distinctive E1-E2 architecture and mechanism in the autophagy pathway. Mol Cell. 44, 451-61
Sangwan, S., Zhao, A., Adams, K. L., Jayson, C. K., Sawaya, M. R., Guenther, E. L., Pan, A. C., Ngo, J., Moore, D. M., Soriaga, A. B., Do, T. D., Goldschmidt, L., Nelson, R., Bowers, M. T., Koehler, C. M., Shaw, D. E., Novitch, B. G., and Eisenberg, D. S. (2017) Atomic structure of a toxic, oligomeric segment of SOD1 linked to amyotrophic lateral sclerosis (ALS). Proc Natl Acad Sci U S A. 114, 8770-8775
Diver, M. M., Pedi, L., Koide, A., Koide, S., and Long, S. B. (2018) Atomic structure of the eukaryotic intramembrane RAS methyltransferase ICMT. Nature. 10.1038/nature25439
Diver, M. M., Pedi, L., Koide, A., Koide, S., and Long, S. B. (2018) Atomic structure of the eukaryotic intramembrane RAS methyltransferase ICMT. Nature. 10.1038/nature25439
Mao, D. Y. L., Neculai, D., Downey, M., Orlicky, S., Haffani, Y. Z., Ceccarelli, D. F., Ho, J. S. L., Szilard, R. K., Zhang, W., Ho, C. S., Wan, L., Fares, C., Rumpel, S., Kurinov, I., Arrowsmith, C. H., Durocher, D., and Sicheri, F. (2008) Atomic structure of the KEOPS complex: an ancient protein kinase-containing molecular machine. Mol Cell. 32, 259-75
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
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
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
Krotee, P., Rodriguez, J. A., Sawaya, M. R., Cascio, D., Reyes, F. E., Shi, D., Hattne, J., Nannenga, B. L., Oskarsson, M. E., Philipp, S., Griner, S., Jiang, L., Glabe, C. G., Westermark, G. T., Gonen, T., and Eisenberg, D. S. (2017) Atomic structures of fibrillar segments of hIAPP suggest tightly mated β-sheets are important for cytotoxicity.. Elife. 10.7554/eLife.19273
Zhang, Y., Kittredge, A., Ward, N., Ji, C., Chen, S., and Yang, T. (2018) ATP activates bestrophin ion channels through direct interaction. Nat Commun. 9, 3126
Cai, R., Price, I. R., Ding, F., Wu, F., Chen, T., Zhang, Y., Liu, G., Jardine, P. J., Lu, C., and Ke, A. (2019) ATP/ADP modulates gp16-pRNA conformational change in the Phi29 DNA packaging motor. Nucleic Acids Res. 10.1093/nar/gkz692
Muok, A. R., Ortega, D. R., Kurniyati, K., Yang, W., Maschmann, Z. A., Mabrouk, A. Sidi, Li, C., Crane, B. R., and Briegel, A. (2020) Atypical chemoreceptor arrays accommodate high membrane curvature. Nat Commun. 11, 5763

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