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Scrima, A., Konícková, R., Czyzewski, B. K., Kawasaki, Y., Jeffrey, P. D., Groisman, R., Nakatani, Y., Iwai, S., Pavletich, N. P., and Thomä, N. H. (2008) Structural basis of UV DNA-damage recognition by the DDB1-DDB2 complex. Cell. 135, 1213-23
Nithianantham, S., Cook, B. D., Beans, M., Guo, F., Chang, F., and Al-Bassam, J. (2018) Structural basis of tubulin recruitment and assembly by microtubule polymerases with Tumor Overexpressed Gene (TOG) domain arrays. Elife. 10.7554/eLife.38922
Dhindwal, S., Gomez-Gil, L., Neau, D. B., Pham, T. Thanh My, Sylvestre, M., Eltis, L. D., Bolin, J. T., and Kumar, P. (2016) Structural Basis of the Enhanced Pollutant-Degrading Capabilities of an Engineered Biphenyl Dioxygenase. J Bacteriol. 198, 1499-512
Armache, K. - J., Garlick, J. D., Canzio, D., Narlikar, G. J., and Kingston, R. E. (2011) Structural basis of silencing: Sir3 BAH domain in complex with a nucleosome at 3.0 Å resolution.. Science. 334, 977-82
Li, J., Wang, L., Hahn, Q., Nowak, R. P., Viennet, T., Orellana, E. A., Burman, S. S. Roy, Yue, H., Hunkeler, M., Fontana, P., Wu, H., Arthanari, H., Fischer, E. S., and Gregory, R. I. (2023) Structural basis of regulated mG tRNA modification by METTL1-WDR4. Nature. 613, 391-397
Dharmaiah, S., Bindu, L., Tran, T. H., Gillette, W. K., Frank, P. H., Ghirlando, R., Nissley, D. V., Esposito, D., McCormick, F., Stephen, A. G., and Simanshu, D. K. (2016) Structural basis of recognition of farnesylated and methylated KRAS4b by PDEδ.. Proc Natl Acad Sci U S A. 113, E6766-E6775
Kumar, S., Athreya, A., Gulati, A., Nair, R. Mony, Mahendran, I., Ranjan, R., and Penmatsa, A. (2021) Structural basis of inhibition of a transporter from Staphylococcus aureus, NorC, through a single-domain camelid antibody. Commun Biol. 4, 836
Lee, S. - J., Ren, F., Zangerl-Plessl, E. - M., Heyman, S., Stary-Weinzinger, A., Yuan, P., and Nichols, C. G. (2016) Structural basis of control of inward rectifier Kir2 channel gating by bulk anionic phospholipids. J Gen Physiol. 148, 227-37
Clayton, G. M., Wang, Y., Crawford, F., Novikov, A., Wimberly, B. T., Kieft, J. S., Falta, M. T., Bowerman, N. A., Marrack, P., Fontenot, A. P., Dai, S., and Kappler, J. W. (2014) Structural basis of chronic beryllium disease: linking allergic hypersensitivity and autoimmunity. Cell. 158, 132-42
Yelshanskaya, M. V., Singh, A. K., Narangoda, C., Williams, R. S. B., Kurnikova, M. G., and Sobolevsky, A. I. (2020) Structural basis of AMPA receptor inhibition by 4-BCCA. Br J Pharmacol. 10.1111/bph.15254
Kozlov, G., Mattijssen, S., Jiang, J., Nyandwi, S., Sprules, T., Iben, J. R., Coon, S. L., Gaidamakov, S., Noronha, A. M., Wilds, C. J., Maraia, R. J., and Gehring, K. (2022) Structural basis of 3'-end poly(A) RNA recognition by LARP1. Nucleic Acids Res. 10.1093/nar/gkac696
Kozlov, G., Mattijssen, S., Jiang, J., Nyandwi, S., Sprules, T., Iben, J. R., Coon, S. L., Gaidamakov, S., Noronha, A. M., Wilds, C. J., Maraia, R. J., and Gehring, K. (2022) Structural basis of 3'-end poly(A) RNA recognition by LARP1. Nucleic Acids Res. 10.1093/nar/gkac696
Nomura, Y., Montemayor, E. J., Virta, J. M., Hayes, S. M., and Butcher, S. E. (2019) Structural basis for the evolution of cyclic phosphodiesterase activity in the U6 snRNA exoribonuclease Usb1. Nucleic Acids Res. 10.1093/nar/gkz1177
Schmier, B. J., Nelersa, C. M., and Malhotra, A. (2017) Structural Basis for the Bidirectional Activity of Bacillus nanoRNase NrnA. Sci Rep. 7, 11085
Westblade, L. F., Campbell, E. A., Pukhrambam, C., Padovan, J. C., Nickels, B. E., Lamour, V., and Darst, S. A. (2010) Structural basis for the bacterial transcription-repair coupling factor/RNA polymerase interaction. Nucleic Acids Res. 38, 8357-69
Seegar, T. C. M., Killingsworth, L. B., Saha, N., Meyer, P. A., Patra, D., Zimmerman, B., Janes, P. W., Rubinstein, E., Nikolov, D. B., Skiniotis, G., Kruse, A. C., and Blacklow, S. C. (2017) Structural Basis for Regulated Proteolysis by the α-Secretase ADAM10.. Cell. 171, 1638-1648.e7
Nguyen, H. An, Hoffer, E. D., Fagan, C. E., Maehigashi, T., and Dunham, C. M. (2023) Structural basis for reduced ribosomal A-site fidelity in response to P-site codon-anticodon mismatches. J Biol Chem. 299, 104608
Nguyen, H. An, Hoffer, E. D., Fagan, C. E., Maehigashi, T., and Dunham, C. M. (2023) Structural basis for reduced ribosomal A-site fidelity in response to P-site codon-anticodon mismatches. bioRxiv. 10.1101/2023.01.28.526049
Yang, Y., Kang, D., Nguyen, L. A., Smithline, Z. B., Pannecouque, C., Zhan, P., Liu, X., and Steitz, T. A. (2018) Structural basis for potent and broad inhibition of HIV-1 RT by thiophene[3,2-]pyrimidine non-nucleoside inhibitors. Elife. 10.7554/eLife.36340
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
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
Nithianantham, S., McNally, F. J., and Al-Bassam, J. (2018) Structural Basis for Disassembly of Katanin Heterododecamers. J Biol Chem. 10.1074/jbc.RA117.001215
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
M Joyce, G., Bu, W., Chen, W. - H., Gillespie, R. A., Andrews, S. F., Wheatley, A. K., Tsybovsky, Y., Jensen, J. L., Stephens, T., Prabhakaran, M., Fisher, B. E., Narpala, S. R., Bagchi, M., McDermott, A. B., Nabel, G. J., Kwong, P. D., Mascola, J. R., Cohen, J. I., and Kanekiyo, M. (2025) Structural basis for complement receptor engagement and virus neutralization through Epstein-Barr virus gp350. Immunity. 58, 295-308.e5
M Joyce, G., Bu, W., Chen, W. - H., Gillespie, R. A., Andrews, S. F., Wheatley, A. K., Tsybovsky, Y., Jensen, J. L., Stephens, T., Prabhakaran, M., Fisher, B. E., Narpala, S. R., Bagchi, M., McDermott, A. B., Nabel, G. J., Kwong, P. D., Mascola, J. R., Cohen, J. I., and Kanekiyo, M. (2025) Structural basis for complement receptor engagement and virus neutralization through Epstein-Barr virus gp350. Immunity. 58, 295-308.e5

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