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Journal Article

Lormand, J. D., Kim, S. - K., Walters-Marrah, G. A., Brownfield, B. A., J Fromme, C., Winkler, W. C., Goodson, J. R., Lee, V. T., and Sondermann, H. (2021) Structural characterization of NrnC identifies unifying features of dinucleotidases. Elife. 10.7554/eLife.70146

Faust, T. B., Yoon, H., Nowak, R. P., Donovan, K. A., Li, Z., Cai, Q., Eleuteri, N. A., Zhang, T., Gray, N. S., and Fischer, E. S. (2020) Structural complementarity facilitates E7820-mediated degradation of RBM39 by DCAF15. Nat Chem Biol. 16, 7-14

Faust, T. B., Yoon, H., Nowak, R. P., Donovan, K. A., Li, Z., Cai, Q., Eleuteri, N. A., Zhang, T., Gray, N. S., and Fischer, E. S. (2020) Structural complementarity facilitates E7820-mediated degradation of RBM39 by DCAF15. Nat Chem Biol. 16, 7-14

Bradley, T., Fera, D., Bhiman, J., Eslamizar, L., Lu, X., Anasti, K., Zhang, R., Sutherland, L. L., Scearce, R. M., Bowman, C. M., Stolarchuk, C., Lloyd, K. E., Parks, R., Eaton, A., Foulger, A., Nie, X., Karim, S. S. Abdool, Barnett, S., Kelsoe, G., Kepler, T. B., S Alam, M., Montefiori, D. C., M Moody, A., Liao, H. - X., Morris, L., Santra, S., Harrison, S. C., and Haynes, B. F. (2016) Structural Constraints of Vaccine-Induced Tier-2 Autologous HIV Neutralizing Antibodies Targeting the Receptor-Binding Site. Cell Rep. 14, 43-54

Bradley, T., Fera, D., Bhiman, J., Eslamizar, L., Lu, X., Anasti, K., Zhang, R., Sutherland, L. L., Scearce, R. M., Bowman, C. M., Stolarchuk, C., Lloyd, K. E., Parks, R., Eaton, A., Foulger, A., Nie, X., Karim, S. S. Abdool, Barnett, S., Kelsoe, G., Kepler, T. B., S Alam, M., Montefiori, D. C., M Moody, A., Liao, H. - X., Morris, L., Santra, S., Harrison, S. C., and Haynes, B. F. (2016) Structural Constraints of Vaccine-Induced Tier-2 Autologous HIV Neutralizing Antibodies Targeting the Receptor-Binding Site. Cell Rep. 14, 43-54

Goris, M., Magin, R. S., Foyn, H., Myklebust, L. M., Varland, S., Ree, R., Drazic, A., Bhambra, P., Støve, S. I., Baumann, M., Haug, B. Erik, Marmorstein, R., and Arnesen, T. (2018) Structural determinants and cellular environment define processed actin as the sole substrate of the N-terminal acetyltransferase NAA80. Proc Natl Acad Sci U S A. 115, 4405-4410

Shek, R., Hilaire, T., Sim, J., and French, J. B. (2019) Structural Determinants for Substrate Selectivity in Guanine Deaminase Enzymes of the Amidohydrolase Superfamily. Biochemistry. 58, 3280-3292

Pruitt, R. N., Chumbler, N. M., Rutherford, S. A., Farrow, M. A., Friedman, D. B., Spiller, B., and D Lacy, B. (2012) Structural determinants of Clostridium difficile toxin A glucosyltransferase activity. J Biol Chem. 287, 8013-20

Pruitt, R. N., Chumbler, N. M., Rutherford, S. A., Farrow, M. A., Friedman, D. B., Spiller, B., and D Lacy, B. (2012) Structural determinants of Clostridium difficile toxin A glucosyltransferase activity. J Biol Chem. 287, 8013-20

Sander, C. L., Luu, J., Kim, K., Furkert, D., Jang, K., Reichenwallner, J., Kang, M. S., Lee, H. - J., Eger, B. T., Choe, H. - W., Fiedler, D., Ernst, O. P., Kim, Y. Ju, Palczewski, K., and Kiser, P. D. (2021) Structural evidence for visual arrestin priming via complexation of phosphoinositols. Structure. 10.1016/j.str.2021.10.002

Sander, C. L., Luu, J., Kim, K., Furkert, D., Jang, K., Reichenwallner, J., Kang, M. S., Lee, H. - J., Eger, B. T., Choe, H. - W., Fiedler, D., Ernst, O. P., Kim, Y. Ju, Palczewski, K., and Kiser, P. D. (2021) Structural evidence for visual arrestin priming via complexation of phosphoinositols. Structure. 10.1016/j.str.2021.10.002

Fribourgh, J. L., Nguyen, H. C., Matreyek, K. A., Alvarez, F. Joan D., Summers, B. J., Dewdney, T. G., Aiken, C., Zhang, P., Engelman, A., and Xiong, Y. (2014) Structural insight into HIV-1 restriction by MxB. Cell Host Microbe. 16, 627-638

Wittenborn, E. C., Cohen, S. E., Merrouch, M., Léger, C., Fourmond, V., Dementin, S., and Drennan, C. L. (2019) Structural insight into metallocofactor maturation in carbon monoxide dehydrogenase. J Biol Chem. 294, 13017-13026

Wang, Y., Feng, H., Zhu, Y., and Gao, P. (2017) Structural insights into glutathione-mediated activation of the master regulator PrfA in Listeria monocytogenes. Protein Cell. 8, 308-312

Viennet, T., Yin, M., Jayaraj, A., Kim, W., Sun, Z. - Y. J., Fujiwara, Y., Zhang, K., Seruggia, D., Seo, H. - S., Dhe-Paganon, S., Orkin, S. H., and Arthanari, H. (2024) Structural insights into the DNA-binding mechanism of BCL11A: The integral role of ZnF6. Structure. 32, 2276-2286.e4

Viennet, T., Yin, M., Jayaraj, A., Kim, W., Sun, Z. - Y. J., Fujiwara, Y., Zhang, K., Seruggia, D., Seo, H. - S., Dhe-Paganon, S., Orkin, S. H., and Arthanari, H. (2024) Structural Insights into the DNA-Binding Mechanism of BCL11A: The Integral Role of ZnF6. bioRxiv. 10.1101/2024.01.17.576058

Zuo, Y., De, S., Feng, Y., and Steitz, T. A. (2020) Structural Insights into Transcription Initiation from De Novo RNA Synthesis to Transitioning into Elongation. iScience. 23, 101445

Fagan, C. E., Maehigashi, T., Dunkle, J. A., Miles, S. J., and Dunham, C. M. (2014) Structural insights into translational recoding by frameshift suppressor tRNASufJ. RNA. 20, 1944-54

Geng, Y., Mosyak, L., Kurinov, I., Zuo, H., Sturchler, E., Cheng, T. Cheung, Subramanyam, P., Brown, A. P., Brennan, S. C., Mun, H. - C., Bush, M., Chen, Y., Nguyen, T. X., Cao, B., Chang, D. D., Quick, M., Conigrave, A. D., Colecraft, H. M., McDonald, P., and Fan, Q. R. (2016) Structural mechanism of ligand activation in human calcium-sensing receptor. Elife. 10.7554/eLife.13662

Geng, Y., Bush, M., Mosyak, L., Wang, F., and Fan, Q. R. (2013) Structural mechanism of ligand activation in human GABA(B) receptor. Nature. 504, 254-9

Frey, K. M., Bertoletti, N., Chan, A. H., Ippolito, J. A., Bollini, M., Spasov, K. A., Jorgensen, W. L., and Anderson, K. S. (2022) Structural Studies and Structure Activity Relationships for Novel Computationally Designed Non-nucleoside Inhibitors and Their Interactions With HIV-1 Reverse Transcriptase. Front Mol Biosci. 9, 805187

Fisher, O. S., Zhang, R., Li, X., Murphy, J. W., Demeler, B., and Boggon, T. J. (2013) Structural studies of cerebral cavernous malformations 2 (CCM2) reveal a folded helical domain at its C-terminus. FEBS Lett. 587, 272-7

Dowling, D. P., Gantt, S. L., Gattis, S. G., Fierke, C. A., and Christianson, D. W. (2008) Structural studies of human histone deacetylase 8 and its site-specific variants complexed with substrate and inhibitors. Biochemistry. 47, 13554-63

Fenwick, M. K., Li, Y., Cresswell, P., Modis, Y., and Ealick, S. E. (2017) Structural studies of viperin, an antiviral radical SAM enzyme. Proc Natl Acad Sci U S A. 10.1073/pnas.1705402114

Tuukkanen, A. T., Freire, D., Chan, S., Arbing, M. A., Reed, R. W., Evans, T. J., Zenkeviciutė, G., Kim, J., Kahng, S., Sawaya, M. R., Chaton, C. T., Wilmanns, M., Eisenberg, D., Parret, A. H. A., and Korotkov, K. V. (2018) Structural Variability of EspG Chaperones from Mycobacterial ESX-1, ESX-3 and ESX-5 Type VII Secretion Systems. J Mol Biol. 10.1016/j.jmb.2018.11.003

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The Northeastern Collaborative Access Team (NE-CAT) facility at the Advanced Photon Source at Argonne National Laboratory is managed by Cornell University and consists of eight member institutions:

Columbia University
Cornell University
Genentech
Harvard University
Memorial Sloan-Kettering Cancer Center
Massachusetts Institute of Technology
Rockefeller University
Yale University

Primary funding for this project comes from the National Institute of General Medical Sciences (NIGMS), a division of the National Institutes of Health (NIH). Additional financial support for NE-CAT comes from the member institutions.