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Newton, A. S., Deiana, L., Puleo, D. E., Cisneros, J. A., Cutrona, K. J., Schlessinger, J., and Jorgensen, W. L. (2017) JAK2 JH2 Fluorescence Polarization Assay and Crystal Structures for Complexes with Three Small Molecules. ACS Med Chem Lett. 8, 614-617
Neumann, W., Xu, S., Sárosi, M. B., Scholz, M. S., Crews, B. C., Ghebreselasie, K., Banerjee, S., Marnett, L. J., and Hey-Hawkins, E. (2016) nido-Dicarbaborate Induces Potent and Selective Inhibition of Cyclooxygenase-2. ChemMedChem. 11, 175-8
Nelson, A. C., Turbyville, T. J., Dharmaiah, S., Rigby, M., Yang, R., Wang, T. - Y., Columbus, J., Stephens, R., Taylor, T., Sciacca, D., Onsongo, G., Sarver, A., Subramanian, S., Nissley, D. V., Simanshu, D. K., and Lou, E. (2020) internal tandem duplication disrupts GTPase-activating protein (GAP) binding to activate oncogenic signaling. J Biol Chem. 10.1074/jbc.RA119.011080
Nelersa, C. M., Schmier, B. J., and Malhotra, A. (2011) Purification and crystallization of Bacillus subtilis NrnA, a novel enzyme involved in nanoRNA degradation. Acta Crystallogr Sect F Struct Biol Cryst Commun. 67, 1235-8
Neau, D., and Perry, K. (2022) Practical Course in Macromolecular Crystallography. 36th Annual Symposium of The Protein Society, July 7-10, 2022
Neau, D. (2014) Recent Developments at NE-CAT, a Macromolecular Crystallography Synchrotron Facility. Indo-US International Conference/Workshop on Recent Advances in Structural Biology and Drug Discovery, October 9-11, 2014
Neau, D. B., Bender, G., Boeglin, W. E., Bartlett, S. G., Brash, A. R., and Newcomer, M. E. (2014) Crystal structure of a lipoxygenase in complex with substrate: the arachidonic acid-binding site of 8R-lipoxygenase. J Biol Chem. 289, 31905-13
Nayak, D., and Sivaraman, J. (2018) Structure of LNX1:Ubc13~Ubiquitin complex reveals the role of additional motifs for the E3 ligase activity of LNX1. J Mol Biol. 10.1016/j.jmb.2018.02.016
Nayak, V., Dessau, M., Kucera, K., Anthony, K., Ledizet, M., and Modis, Y. (2009) Crystal structure of dengue virus type 1 envelope protein in the postfusion conformation and its implications for membrane fusion. J Virol. 83, 4338-44
Nayak, D., Lv, D., Yuan, Y., Zhang, P., Hu, W., Nayak, A., Ruben, E. A., Lv, Z., Sung, P., Hromas, R., Zheng, G., Zhou, D., and Olsen, S. K. (2024) Development and crystal structures of a potent second-generation dual degrader of BCL-2 and BCL-xL. Nat Commun. 15, 2743
Narui, Y., and Sotomayor, M. (2018) Tuning Inner-Ear Tip-Link Affinity Through Alternatively Spliced Variants of Protocadherin-15. Biochemistry. 10.1021/acs.biochem.7b01075
Nandakumar, J., Shuman, S., and Lima, C. D. (2006) RNA ligase structures reveal the basis for RNA specificity and conformational changes that drive ligation forward. Cell. 127, 71-84
Nandakumar, J., Nair, P. A., and Shuman, S. (2007) Last stop on the road to repair: structure of E. coli DNA ligase bound to nicked DNA-adenylate. Mol Cell. 26, 257-71
Nam, K. Hyun, Haitjema, C., Liu, X., Ding, F., Wang, H., DeLisa, M. P., and Ke, A. (2012) Cas5d protein processes pre-crRNA and assembles into a cascade-like interference complex in subtype I-C/Dvulg CRISPR-Cas system. Structure. 20, 1574-84
Nam, D., Bacik, J. - P., Khade, R. L., Aguilera, M. Camila, Wei, Y., Villada, J. D., Neidig, M. L., Zhang, Y., Ando, N., and Fasan, R. (2023) Mechanistic manifold in a hemoprotein-catalyzed cyclopropanation reaction with diazoketone. Nat Commun. 14, 7985
Nam, Y., Chen, C., Gregory, R. I., Chou, J. J., and Sliz, P. (2011) Molecular basis for interaction of let-7 microRNAs with Lin28. Cell. 147, 1080-91
Nam, K. Hyun, Kurinov, I., and Ke, A. (2011) Crystal structure of clustered regularly interspaced short palindromic repeats (CRISPR)-associated Csn2 protein revealed Ca2+-dependent double-stranded DNA binding activity. J Biol Chem. 286, 30759-68
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
Nakashige, T. G., Zygiel, E. M., Drennan, C. L., and Nolan, E. M. (2017) Nickel Sequestration by the Host-Defense Protein Human Calprotectin. J Am Chem Soc. 10.1021/jacs.7b01212
Nakashige, T. G., Bowman, S. E. J., Zygiel, E. M., Drennan, C. L., and Nolan, E. M. (2018) Biophysical Examination of the Calcium-Modulated Nickel-Binding Properties of Human Calprotectin Reveals Conformational Change in the EF-Hand Domains and HisAsp Site. Biochemistry. 10.1021/acs.biochem.8b00415
Nakanishi, K., Weinberg, D. E., Bartel, D. P., and Patel, D. J. (2012) Structure of yeast Argonaute with guide RNA. Nature. 486, 368-74
Nakanishi, K., Ascano, M., Gogakos, T., Ishibe-Murakami, S., Serganov, A. A., Briskin, D., Morozov, P., Tuschl, T., and Patel, D. J. (2013) Eukaryote-specific insertion elements control human ARGONAUTE slicer activity. Cell Rep. 3, 1893-900
Nair, P. A., Nandakumar, J., Smith, P., Odell, M., Lima, C. D., and Shuman, S. (2007) Structural basis for nick recognition by a minimal pluripotent DNA ligase. Nat Struct Mol Biol. 14, 770-8
Nabel, K. G., Clark, S. A., Shankar, S., Pan, J., Clark, L. E., Yang, P., Coscia, A., McKay, L. G. A., Varnum, H. H., Brusic, V., Tolan, N. V., Zhou, G., Desjardins, M., Turbett, S. E., Kanjilal, S., Sherman, A. C., Dighe, A., LaRocque, R. C., Ryan, E. T., Tylek, C., Cohen-Solal, J. F., Darcy, A. T., Tavella, D., Clabbers, A., Fan, Y., Griffiths, A., Correia, I. R., Seagal, J., Baden, L. R., Charles, R. C., and Abraham, J. (2021) Structural basis for continued antibody evasion by the SARS-CoV-2 receptor binding domain. Science

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