Publications

Found 1265 results
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Journal Article
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
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
Rajagopalan, S., Teter, S. J., Zwart, P. H., Brennan, R. G., Phillips, K. J., and Kiley, P. J. (2013) Studies of IscR reveal a unique mechanism for metal-dependent regulation of DNA binding specificity. Nat Struct Mol Biol. 20, 740-7
Knappenberger, A. John, Reiss, C. Wetheringt, and Strobel, S. A. (2018) Structures of two aptamers with differing ligand specificity reveal ruggedness in the functional landscape of RNA. Elife. 10.7554/eLife.36381
Su, C. - C., Klenotic, P. A., Cui, M., Lyu, M., Morgan, C. E., and Yu, E. W. (2021) Structures of the mycobacterial membrane protein MmpL3 reveal its mechanism of lipid transport. PLoS Biol. 19, e3001370
Dunkle, J. A., Wang, L., Feldman, M. B., Pulk, A., Chen, V. B., Kapral, G. J., Noeske, J., Richardson, J. S., Blanchard, S. C., and Cate, J. H. Doudna (2011) Structures of the bacterial ribosome in classical and hybrid states of tRNA binding. Science. 332, 981-4
Anand, R., Kaminski, P. Alexandre, and Ealick, S. E. (2004) Structures of purine 2'-deoxyribosyltransferase, substrate complexes, and the ribosylated enzyme intermediate at 2.0 A resolution. Biochemistry. 43, 2384-93
Berman, A. J., Kamtekar, S., Goodman, J. L., Lázaro, J. M., de Vega, M., Blanco, L., Salas, M., and Steitz, T. A. (2007) Structures of phi29 DNA polymerase complexed with substrate: the mechanism of translocation in B-family polymerases. EMBO J. 26, 3494-505
Kuzina, E. S., Ung, P. Man- Un, Mohanty, J., Tome, F., Choi, J., Pardon, E., Steyaert, J., Lax, I., Schlessinger, A., Schlessinger, J., and Lee, S. (2019) Structures of ligand-occupied β-Klotho complexes reveal a molecular mechanism underlying endocrine FGF specificity and activity.. Proc Natl Acad Sci U S A. 116, 7819-7824
Wagner, J. M., Chan, S., Evans, T. J., Kahng, S., Kim, J., Arbing, M. A., Eisenberg, D., and Korotkov, K. V. (2016) Structures of EccB1 and EccD1 from the core complex of the mycobacterial ESX-1 type VII secretion system. BMC Struct Biol. 16, 5
Wagner, J. M., Chan, S., Evans, T. J., Kahng, S., Kim, J., Arbing, M. A., Eisenberg, D., and Korotkov, K. V. (2016) Structures of EccB1 and EccD1 from the core complex of the mycobacterial ESX-1 type VII secretion system. BMC Struct Biol. 16, 5
Wagner, J. M., Chan, S., Evans, T. J., Kahng, S., Kim, J., Arbing, M. A., Eisenberg, D., and Korotkov, K. V. (2016) Structures of EccB1 and EccD1 from the core complex of the mycobacterial ESX-1 type VII secretion system. BMC Struct Biol. 16, 5
Eaglesham, J. B., McCarty, K. L., and Kranzusch, P. J. (2020) Structures of diverse poxin cGAMP nucleases reveal a widespread role for cGAS-STING evasion in host-pathogen conflict. Elife. 10.7554/eLife.59753
Huo, Y., Nam, K. Hyun, Ding, F., Lee, H., Wu, L., Xiao, Y., M Farchione, D., Zhou, S., Rajashankar, K., Kurinov, I., Zhang, R., and Ke, A. (2014) Structures of CRISPR Cas3 offer mechanistic insights into Cascade-activated DNA unwinding and degradation. Nat Struct Mol Biol. 21, 771-7

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