Publications

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Journal Article
Sukumar, N., Dewanti, A., Merli, A., Rossi, G. Luigi, Mitra, B., and F Mathews, S. (2009) Structures of the G81A mutant form of the active chimera of (S)-mandelate dehydrogenase and its complex with two of its substrates. Acta Crystallogr D Biol Crystallogr. 65, 543-52
Zhang, W., Dunkle, J. A., and Cate, J. H. D. (2009) Structures of the ribosome in intermediate states of ratcheting. Science. 325, 1014-7
F Demircioglu, E., Sosa, B. A., Ingram, J., Ploegh, H. L., and Schwartz, T. U. (2016) Structures of TorsinA and its disease-mutant complexed with an activator reveal the molecular basis for primary dystonia. Elife. 10.7554/eLife.17983
Blank, P. N., Barrow, G. H., Chou, W. K. W., Duan, L., Cane, D. E., and Christianson, D. W. (2017) Substitution of Aromatic Residues with Polar Residues in the Active Site Pocket of epi-Isozizaene Synthase Leads to the Generation of New Cyclic Sesquiterpenes. Biochemistry. 10.1021/acs.biochem.7b00895
Blus, B. J., Hashimoto, H., Seo, H. - S., Krolak, A., and Debler, E. W. (2019) Substrate Affinity and Specificity of the ScSth1p Bromodomain Are Fine-Tuned for Versatile Histone Recognition. Structure. 27, 1460-1468.e3
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
Rosenberg, O. S., Dovala, D., Li, X., Connolly, L., Bendebury, A., Finer-Moore, J., Holton, J., Cheng, Y., Stroud, R. M., and Cox, J. S. (2015) Substrates Control Multimerization and Activation of the Multi-Domain ATPase Motor of Type VII Secretion. Cell. 161, 501-512
Leibly, D. J., Arbing, M. A., Pashkov, I., DeVore, N., Waldo, G. S., Terwilliger, T. C., and Yeates, T. O. (2015) A Suite of Engineered GFP Molecules for Oligomeric Scaffolding. Structure. 23, 1754-1768
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
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
Pecic, S., Pakhomova, S., Newcomer, M. E., Morisseau, C., Hammock, B. D., Zhu, Z., Rinderspacher, A., and Deng, S. - X. (2013) Synthesis and structure-activity relationship of piperidine-derived non-urea soluble epoxide hydrolase inhibitors. Bioorg Med Chem Lett. 23, 417-21
Morris, W., Volosskiy, B., Demir, S., Gándara, F., McGrier, P. L., Furukawa, H., Cascio, D., J Stoddart, F., and Yaghi, O. M. (2012) Synthesis, structure, and metalation of two new highly porous zirconium metal-organic frameworks. Inorg Chem. 51, 6443-5
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
Carlson, A. S., Cui, H., Divakaran, A., Johnson, J. A., Brunner, R. M., Pomerantz, W. C. K., and Topczewski, J. J. (2019) Systematically Mitigating the p38α Activity of Triazole-based BET Inhibitors.. ACS Med Chem Lett. 10, 1296-1301
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
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
Zimanyi, C. M., Ando, N., Brignole, E. J., Asturias, F. J., Stubbe, J. A., and Drennan, C. L. (2012) Tangled up in knots: structures of inactivated forms of E. coli class Ia ribonucleotide reductase. Structure. 20, 1374-83
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
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
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
Vemulapalli, V., Donovan, K. A., Seegar, T. C. M., Rogers, J. M., Bae, M., Lumpkin, R. J., Cao, R., Henke, M. T., Ray, S. S., Fischer, E. S., Cuny, G. D., and Blacklow, S. C. (2021) Targeted Degradation of the Oncogenic Phosphatase SHP2. Biochemistry. 60, 2593-2609
De Schutter, J. W., Morrison, J. P., Morrison, M. J., Ciulli, A., and Imperiali, B. (2017) Targeting Bacillosamine Biosynthesis in Bacterial Pathogens: Development of Inhibitors to a Bacterial Amino-Sugar Acetyltransferase from Campylobacter jejuni. J Med Chem. 60, 2099-2118

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