Publications

Found 826 results
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Journal Article
Tu, D., Graziano, B. R., Park, E., Zheng, W., Li, Y., Goode, B. L., and Eck, M. J. (2012) Structure of the formin-interaction domain of the actin nucleation-promoting factor Bud6. Proc Natl Acad Sci U S A. 109, E3424-33
Papadopoulos, E., Jenni, S., Kabha, E., Takrouri, K. J., Yi, T., Salvi, N., Luna, R. E., Gavathiotis, E., Mahalingam, P., Arthanari, H., Rodriguez-Mias, R., Yefidoff-Freedman, R., Aktas, B. H., Chorev, M., Halperin, J. A., and Wagner, G. (2014) Structure of the eukaryotic translation initiation factor eIF4E in complex with 4EGI-1 reveals an allosteric mechanism for dissociating eIF4G. Proc Natl Acad Sci U S A. 111, E3187-95
Chitrakar, I., Ahmed, S. Fardin, Torelli, A. T., and French, J. B. (2021) Structure of the E. coli agmatinase, SPEB. PLoS One. 16, e0248991
Mahoney, B. J., Takayesu, A., Zhou, A., Cascio, D., and Clubb, R. T. (2022) The structure of the Clostridium thermocellum RsgI9 ectodomain provides insight into the mechanism of biomass sensing. Proteins. 10.1002/prot.26326
Galaleldeen, A., Taylor, A. B., Chen, D., Schuermann, J. P., Holloway, S. P., Hou, S., Gong, S., Zhong, G., and P Hart, J. (2013) Structure of the Chlamydia trachomatis immunodominant antigen Pgp3. J Biol Chem. 288, 22068-79
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
Aoki, S. T., Settembre, E. C., Trask, S. D., Greenberg, H. B., Harrison, S. C., and Dormitzer, P. R. (2009) Structure of rotavirus outer-layer protein VP7 bound with a neutralizing Fab. Science. 324, 1444-7
Makde, R. D., England, J. R., Yennawar, H. P., and Tan, S. (2010) Structure of RCC1 chromatin factor bound to the nucleosome core particle. Nature. 467, 562-6
Brugger, C., Schwartz, J., Novick, S., Tong, S., Hoskins, J., Majdalani, N., Kim, R., Filipovski, M., Wickner, S., Gottesman, S., Griffin, P., and Deaconescu, A. M. (2023) Structure of Phosphorylated-like RssB, the Adaptor Delivering σ to the ClpXP Proteolytic Machinery, Reveals an Interface Switch for Activation.. J Biol Chem. 10.1016/j.jbc.2023.105440
Chen, E., Trajkovski, M., Lee, H. Kyung, Nyovanie, S., Martin, K. N., Dean, W. L., Tahiliani, M., Plavec, J., and Yatsunyk, L. A. (2024) Structure of native four-repeat satellite III sequence with non-canonical base interactions. Nucleic Acids Res. 52, 3390-3405
Chen, E., Trajkovski, M., Lee, H. Kyung, Nyovanie, S., Martin, K. N., Dean, W. L., Tahiliani, M., Plavec, J., and Yatsunyk, L. A. (2024) Structure of native four-repeat satellite III sequence with non-canonical base interactions. Nucleic Acids Res. 52, 3390-3405
Tabackman, A. A., Frankson, R., Marsan, E. S., Perry, K., and Cole, K. E. (2016) Structure of 'linkerless' hydroxamic acid inhibitor-HDAC8 complex confirms the formation of an isoform-specific subpocket. J Struct Biol. 195, 373-378
Zhao, Q., Han, Q., Kissinger, C. R., Hermann, T., and Thompson, P. A. (2008) Structure of hepatitis C virus IRES subdomain IIa. Acta Crystallogr D Biol Crystallogr. 64, 436-43
Zoltowski, B. D., Vaidya, A. T., Top, D., Widom, J., Young, M. W., and Crane, B. R. (2011) Structure of full-length Drosophila cryptochrome. Nature. 480, 396-9
Khabibullina, N. F., Tereshchenkov, A. G., Komarova, E. S., Syroegin, E. A., Shiriaev, D. I., Paleskava, A., Kartsev, V. G., Bogdanov, A. A., Konevega, A. L., Dontsova, O. A., Sergiev, P. V., Osterman, I. A., and Polikanov, Y. S. (2019) Structure of dirithromycin bound to the bacterial ribosome suggests new ways for rational improvement of macrolides. Antimicrob Agents Chemother. 10.1128/AAC.02266-18
Mehboob, S., Mulhearn, D. C., Truong, K., Johnson, M. E., and Santarsiero, B. D. (2010) Structure of dihydroorotase from Bacillus anthracis at 2.6 Å resolution.. Acta Crystallogr Sect F Struct Biol Cryst Commun. 66, 1432-5
Becker, A., Kannan, T. R., Taylor, A. B., Pakhomova, O. N., Zhang, Y., Somarajan, S. R., Galaleldeen, A., Holloway, S. P., Baseman, J. B., and P Hart, J. (2015) Structure of CARDS toxin, a unique ADP-ribosylating and vacuolating cytotoxin from Mycoplasma pneumoniae. Proc Natl Acad Sci U S A. 112, 5165-70
Mi, L. - Z., Brown, C. T., Gao, Y., Tian, Y., Le, V. Q., Walz, T., and Springer, T. A. (2015) Structure of bone morphogenetic protein 9 procomplex. Proc Natl Acad Sci U S A. 112, 3710-5
Schuermann, J. P., Tan, A., Tanner, J. J., and Henzl, M. T. (2010) Structure of avian thymic hormone, a high-affinity avian beta-parvalbumin, in the Ca2+-free and Ca2+-bound states. J Mol Biol. 397, 991-1002
Schuermann, J. P., Tan, A., Tanner, J. J., and Henzl, M. T. (2010) Structure of avian thymic hormone, a high-affinity avian beta-parvalbumin, in the Ca2+-free and Ca2+-bound states. J Mol Biol. 397, 991-1002
Tyler, R. C., Bitto, E., Berndsen, C. E., Bingman, C. A., Singh, S., Lee, M. S., Wesenberg, G. E., Denu, J. M., Phillips, G. N., and Markley, J. L. (2006) Structure of Arabidopsis thaliana At1g77540 protein, a minimal acetyltransferase from the COG2388 family. Biochemistry. 45, 14325-36
Keszei, A. F. A., Tang, X., McCormick, C., Zeqiraj, E., Rohde, J. R., Tyers, M., and Sicheri, F. (2014) Structure of an SspH1-PKN1 complex reveals the basis for host substrate recognition and mechanism of activation for a bacterial E3 ubiquitin ligase. Mol Cell Biol. 34, 362-73
Keszei, A. F. A., Tang, X., McCormick, C., Zeqiraj, E., Rohde, J. R., Tyers, M., and Sicheri, F. (2014) Structure of an SspH1-PKN1 complex reveals the basis for host substrate recognition and mechanism of activation for a bacterial E3 ubiquitin ligase. Mol Cell Biol. 34, 362-73
Wang, Y., Juranek, S., Li, H., Sheng, G., Tuschl, T., and Patel, D. J. (2008) Structure of an argonaute silencing complex with a seed-containing guide DNA and target RNA duplex. Nature. 456, 921-6
Benavides, B. S., Valandro, S., Cioloboc, D., Taylor, A. B., Schanze, K. S., and Kurtz, D. M. (2020) Structure of a Zinc Porphyrin-Substituted Bacterioferritin and Photophysical Properties of Iron Reduction. Biochemistry. 59, 1618-1629

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