Publications

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Journal Article
Siegel, S. D., Amer, B. R., Wu, C., Sawaya, M. R., Gosschalk, J. E., Clubb, R. T., and Ton-That, H. (2019) Structure and Mechanism of LcpA, a Phosphotransferase That Mediates Glycosylation of a Gram-Positive Bacterial Cell Wall-Anchored Protein. MBio. 10.1128/mBio.01580-18
Rechkoblit, O., Gupta, Y. K., Malik, R., Rajashankar, K. R., Johnson, R. E., Prakash, L., Prakash, S., and Aggarwal, A. K. (2016) Structure and mechanism of human PrimPol, a DNA polymerase with primase activity. Sci Adv. 2, e1601317
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
Remus, B. S., Jacewicz, A., and Shuman, S. (2014) Structure and mechanism of E. coli RNA 2',3'-cyclic phosphodiesterase. RNA. 20, 1697-705
Park, E., Kim, N., Ficarro, S. B., Zhang, Y., Lee, B. Il, Cho, A., Kim, K., Park, A. K. J., Park, W. - Y., Murray, B., Meyerson, M., Beroukhim, R., Marto, J. A., Cho, J., and Eck, M. J. (2015) Structure and mechanism of activity-based inhibition of the EGF receptor by Mig6. Nat Struct Mol Biol. 22, 703-711
Sanches, M., Duffy, N. M., Talukdar, M., Thevakumaran, N., Chiovitti, D., Canny, M. D., Lee, K., Kurinov, I., Uehling, D., Al-awar, R., Poda, G., Prakesch, M., Wilson, B., Tam, V., Schweitzer, C., Toro, A., Lucas, J. L., Vuga, D., Lehmann, L., Durocher, D., Zeng, Q., Patterson, J. B., and Sicheri, F. (2014) Structure and mechanism of action of the hydroxy-aryl-aldehyde class of IRE1 endoribonuclease inhibitors. Nat Commun. 5, 4202
Deng, S., Magin, R. S., Wei, X., Pan, B., E Petersson, J., and Marmorstein, R. (2019) Structure and Mechanism of Acetylation by the N-Terminal Dual Enzyme NatA/Naa50 Complex. Structure. 27, 1057-1070.e4
Shen, J., Wu, G., Tsai, A. - L., and Zhou, M. (2020) Structure and Mechanism of a Unique Diiron Center in Mammalian Stearoyl-CoA Desaturase. J Mol Biol. 432, 5152-5161
Lau, R. K., Ye, Q., Birkholz, E. A., Berg, K. R., Patel, L., Mathews, I. T., Watrous, J. D., Ego, K., Whiteley, A. T., Lowey, B., Mekalanos, J. J., Kranzusch, P. J., Jain, M., Pogliano, J., and Corbett, K. D. (2020) Structure and Mechanism of a Cyclic Trinucleotide-Activated Bacterial Endonuclease Mediating Bacteriophage Immunity. Mol Cell. 10.1016/j.molcel.2019.12.010
Singh, M., Wang, Z., Cascio, D., and Feigon, J. (2015) Structure and interactions of the CS domain of human H/ACA RNP assembly protein Shq1. J Mol Biol. 427, 807-23
Dickson, V. Kane, Pedi, L., and Long, S. B. (2014) Structure and insights into the function of a Ca(2+)-activated Cl(-) channel. Nature. 516, 213-8
Wheatley, N. M., Sundberg, C. D., Gidaniyan, S. D., Cascio, D., and Yeates, T. O. (2014) Structure and identification of a pterin dehydratase-like protein as a ribulose-bisphosphate carboxylase/oxygenase (RuBisCO) assembly factor in the α-carboxysome.. J Biol Chem. 289, 7973-81
Singh, M., Gonzales, F. A., Cascio, D., Heckmann, N., Chanfreau, G., and Feigon, J. (2009) Structure and functional studies of the CS domain of the essential H/ACA ribonucleoparticle assembly protein SHQ1. J Biol Chem. 284, 1906-16
Trachman, R. J., Autour, A., C Y Jeng, S., Abdolahzadeh, A., Andreoni, A., Cojocaru, R., Garipov, R., Dolgosheina, E. V., Knutson, J. R., Ryckelynck, M., Unrau, P. J., and Ferré-D'Amaré, A. R. (2019) Structure and functional reselection of the Mango-III fluorogenic RNA aptamer. Nat Chem Biol. 15, 472-479
Geng, Y., Xiong, D., Mosyak, L., Malito, D. L., Kniazeff, J., Chen, Y., Burmakina, S., Quick, M., Bush, M., Javitch, J. A., Pin, J. - P., and Fan, Q. R. (2012) Structure and functional interaction of the extracellular domain of human GABA(B) receptor GBR2. Nat Neurosci. 15, 970-8
Doamekpor, S. K., Lee, J. - W., Hepowit, N. L., Wu, C., Charenton, C., Leonard, M., Bengtson, M. H., Rajashankar, K. R., Sachs, M. S., Lima, C. D., and Joazeiro, C. A. P. (2016) Structure and function of the yeast listerin (Ltn1) conserved N-terminal domain in binding to stalled 60S ribosomal subunits. Proc Natl Acad Sci U S A. 113, E4151-60
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
Hamill, S., Wolin, S. L., and Reinisch, K. M. (2010) Structure and function of the polymerase core of TRAMP, a RNA surveillance complex. Proc Natl Acad Sci U S A. 107, 15045-50
De Ioannes, P., Leon, V. A., Kuang, Z., Wang, M., Boeke, J. D., Hochwagen, A., and Armache, K. - J. (2019) Structure and function of the Orc1 BAH-nucleosome complex. Nat Commun. 10, 2894
Hubin, E. A., Fay, A., Xu, C., Bean, J. M., Saecker, R. M., Glickman, M. S., Darst, S. A., and Campbell, E. A. (2017) Structure and function of the mycobacterial transcription initiation complex with the essential regulator RbpA. Elife. 10.7554/eLife.22520
Zheng, J., Sagar, V., Smolinsky, A., Bourke, C., LaRonde-LeBlanc, N., and T Cropp, A. (2009) Structure and function of the macrolide biosensor protein, MphR(A), with and without erythromycin. J Mol Biol. 387, 1250-60
Vizcarra, C. L., Kreutz, B., Rodal, A. A., Toms, A. V., Lu, J., Zheng, W., Quinlan, M. E., and Eck, M. J. (2011) Structure and function of the interacting domains of Spire and Fmn-family formins. Proc Natl Acad Sci U S A. 108, 11884-9
Osko, J. D., Roose, B. W., Shinsky, S. A., and Christianson, D. W. (2019) Structure and Function of the Acetylpolyamine Amidohydrolase from the Deep Earth Halophile . Biochemistry. 58, 3755-3766
Gaynes, M. N., Osika, K. R., and Christianson, D. W. (2024) Structure and Function of Sabinene Synthase, a Monoterpene Cyclase That Generates a Highly Strained [3.1.0] Bicyclic Product. Biochemistry. 63, 3147-3159
Feld, G. K., El-Etr, S., Corzett, M. H., Hunter, M. S., Belhocine, K., Monack, D. M., Frank, M., Segelke, B. W., and Rasley, A. (2014) Structure and function of REP34 implicates carboxypeptidase activity in Francisella tularensis host cell invasion. J Biol Chem. 289, 30668-30679

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