Publications

Found 453 results
Filters: First Letter Of Last Name is N  [Clear All Filters]
A B C D E F G H I J K L M N O P Q R S T U V W X Y Z 
S
Krishnan, V., Dwivedi, P., Kim, B. J., Samal, A., Macon, K., Ma, X., Mishra, A., Doran, K. S., Ton-That, H., and Narayana, S. V. L. (2013) Structure of Streptococcus agalactiae tip pilin GBS104: a model for GBS pili assembly and host interactions. Acta Crystallogr D Biol Crystallogr. 69, 1073-89
Jobichen, C., Chong, T. Ying, Prabhakar, M. Tirumuru, Nayak, D., Biswas, D., Pannu, N. Singh, Hanski, E., and Sivaraman, J. (2018) Structure of ScpC, a virulence protease from , reveal the functional domains and maturation mechanism. Biochem J. 10.1042/BCJ20180145
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
Lazarus, M. B., Nam, Y., Jiang, J., Sliz, P., and Walker, S. (2011) Structure of human O-GlcNAc transferase and its complex with a peptide substrate. Nature. 469, 564-7
Gilbert, N. C., Bartlett, S. G., Waight, M. T., Neau, D. B., Boeglin, W. E., Brash, A. R., and Newcomer, M. E. (2011) The structure of human 5-lipoxygenase. Science. 331, 217-9
Gilbert, N. C., Bartlett, S. G., Waight, M. T., Neau, D. B., Boeglin, W. E., Brash, A. R., and Newcomer, M. E. (2011) The structure of human 5-lipoxygenase. Science. 331, 217-9
Kobe, M. J., Neau, D. B., Mitchell, C. E., Bartlett, S. G., and Newcomer, M. E. (2014) The structure of human 15-lipoxygenase-2 with a substrate mimic. J Biol Chem. 289, 8562-9
Kobe, M. J., Neau, D. B., Mitchell, C. E., Bartlett, S. G., and Newcomer, M. E. (2014) The structure of human 15-lipoxygenase-2 with a substrate mimic. J Biol Chem. 289, 8562-9
Duda, D. M., Olszewski, J. L., Schuermann, J. P., Kurinov, I., Miller, D. J., Nourse, A., Alpi, A. F., and Schulman, B. A. (2013) Structure of HHARI, a RING-IBR-RING ubiquitin ligase: autoinhibition of an Ariadne-family E3 and insights into ligation mechanism. Structure. 21, 1030-41
Ren, Z., Lee, J., Moosa, M. Muhammad, Nian, Y., Hu, L., Xu, Z., McCoy, J. G., Ferreon, A. Chris M., Im, W., and Zhou, M. (2018) Structure of an EIIC sugar transporter trapped in an inward-facing conformation. Proc Natl Acad Sci U S A. 10.1073/pnas.1800647115
Schauder, C. M., Wu, X., Saheki, Y., Narayanaswamy, P., Torta, F., Wenk, M. R., De Camilli, P., and Reinisch, K. M. (2014) Structure of a lipid-bound extended synaptotagmin indicates a role in lipid transfer. Nature. 510, 552-5
Vasan, N., Hutagalung, A., Novick, P., and Reinisch, K. M. (2010) Structure of a C-terminal fragment of its Vps53 subunit suggests similarity of Golgi-associated retrograde protein (GARP) complex to a family of tethering complexes. Proc Natl Acad Sci U S A. 107, 14176-81
Zimmer, J., Nam, Y., and Rapoport, T. A. (2008) Structure of a complex of the ATPase SecA and the protein-translocation channel. Nature. 455, 936-43
Eek, P., Järving, R., Järving, I., Gilbert, N. C., Newcomer, M. E., and Samel, N. (2012) Structure of a calcium-dependent 11R-lipoxygenase suggests a mechanism for Ca2+ regulation. J Biol Chem. 287, 22377-86
Vigdorovich, V., Ramagopal, U. A., Lázár-Molnár, E., Sylvestre, E., Lee, J. Sik, Hofmeyer, K. A., Zang, X., Nathenson, S. G., and Almo, S. C. (2013) Structure and T cell inhibition properties of B7 family member, B7-H3. Structure. 21, 707-17
Swofford, C. A., Nordeen, S. A., Chen, L., Desai, M. M., Chen, J., Springs, S. L., Schwartz, T. U., and Sinskey, A. J. (2022) Structure and Specificity of an Anti-Chloramphenicol Single Domain Antibody for Detection of Amphenicol Residues. Protein Sci. 10.1002/pro.4457
Nicoludis, J. M., Lau, S. - Y., Schärfe, C. P. I., Marks, D. S., Weihofen, W. A., and Gaudet, R. (2015) Structure and Sequence Analyses of Clustered Protocadherins Reveal Antiparallel Interactions that Mediate Homophilic Specificity. Structure. 23, 2087-98
Horton, J. R., Nugent, R. L., Li, A., Mabuchi, M. Yamada, Fomenkov, A., Cohen-Karni, D., Griggs, R. M., Zhang, X., Wilson, G. G., Zheng, Y., Xu, S. - Y., and Cheng, X. (2014) Structure and mutagenesis of the DNA modification-dependent restriction endonuclease AspBHI. Sci Rep. 4, 4246
Guo, X., Schmiege, P., Assafa, T. E., Wang, R., Xu, Y., Donnelly, L., Fine, M., Ni, X., Jiang, J., Millhauser, G., Feng, L., and Li, X. (2022) Structure and mechanism of human cystine exporter cystinosin. Cell. 185, 3739-3752.e18
Soule, J., Gnann, A. D., Gonzalez, R., Parker, M. J., McKenna, K. C., Nguyen, S. V., Phan, N. T., Wicht, D. K., and Dowling, D. P. (2019) Structure and function of the two-component flavin-dependent methanesulfinate monooxygenase within bacterial sulfur assimilation. Biochem Biophys Res Commun. 10.1016/j.bbrc.2019.11.008
Valentino, H., Campbell, A. C., Schuermann, J. P., Sultana, N., Nam, H. G., LeBlanc, S., Tanner, J. J., and Sobrado, P. (2020) Structure and function of a flavin-dependent S-monooxygenase from garlic (). J Biol Chem. 295, 11042-11055
Barton, W. A., Liu, B. P., Tzvetkova, D., Jeffrey, P. D., Fournier, A. E., Sah, D., Cate, R., Strittmatter, S. M., and Nikolov, D. B. (2003) Structure and axon outgrowth inhibitor binding of the Nogo-66 receptor and related proteins. EMBO J. 22, 3291-302
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
Yan, W., Markegard, E., Dharmaiah, S., Urisman, A., Drew, M., Esposito, D., Scheffzek, K., Nissley, D. V., McCormick, F., and Simanshu, D. K. (2020) Structural Insights into the SPRED1-Neurofibromin-KRAS Complex and Disruption of SPRED1-Neurofibromin Interaction by Oncogenic EGFR. Cell Rep. 32, 107909
Jensen, J. L., Indurthi, V. S. K., Neau, D. B., Vetter, S. W., and Colbert, C. L. (2015) Structural insights into the binding of the human receptor for advanced glycation end products (RAGE) by S100B, as revealed by an S100B-RAGE-derived peptide complex. Acta Crystallogr D Biol Crystallogr. 71, 1176-83

Pages