Publications

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C
Wei, Y., Funk, M. A., Rosado, L. A., Baek, J., Drennan, C. L., and Stubbe, J. A. (2014) The class III ribonucleotide reductase from Neisseria bacilliformis can utilize thioredoxin as a reductant. Proc Natl Acad Sci U S A. 111, E3756-65
Mawla, G. D., Hall, B. M., Cárcamo-Oyarce, G., Grant, R. A., Zhang, J. Jia, Kardon, J. R., Ribbeck, K., Sauer, R. T., and Baker, T. A. (2020) ClpP1P2 peptidase activity promotes biofilm formation in P. aeruginosa. Mol Microbiol. 10.1111/mmi.14649
Li, X., Saha, P., Li, J., Blobel, G., and Pfeffer, S. R. (2016) Clues to the mechanism of cholesterol transfer from the structure of NPC1 middle lumenal domain bound to NPC2. Proc Natl Acad Sci U S A. 113, 10079-84
Rajakulendran, T., Sahmi, M., Kurinov, I., Tyers, M., Therrien, M., and Sicheri, F. (2008) CNK and HYP form a discrete dimer by their SAM domains to mediate RAF kinase signaling. Proc Natl Acad Sci U S A. 105, 2836-41
Maisonneuve, P., Sahmi, M., Bergeron-Labrecque, F., Ma, X. Iris, Queguiner, J., Arseneault, G., Lefrançois, M., Kurinov, I., Fronzes, R., Sicheri, F., and Therrien, M. (2024) The CNK-HYP scaffolding complex promotes RAF activation by enhancing KSR-MEK interaction. Nat Struct Mol Biol. 10.1038/s41594-024-01233-6
Anderson, A. J., Dodge, G. J., Allen, K. N., and Imperiali, B. (2023) Co-conserved sequence motifs are predictive of substrate specificity in a family of monotopic phosphoglycosyl transferases. Protein Sci. 32, e4646
Zhang, J., and Ferré-D'Amaré, A. R. (2013) Co-crystal structure of a T-box riboswitch stem I domain in complex with its cognate tRNA. Nature. 500, 363-6
Kimani, S. W., Perveen, S., Szewezyk, M., Zeng, H., Dong, A., Li, F., Ghiabi, P., Li, Y., Chau, I., Arrowsmith, C. H., Barsyte-Lovejoy, D., Santhakumar, V., Vedadi, M., and Halabelian, L. (2023) The co-crystal structure of Cbl-b and a small-molecule inhibitor reveals the mechanism of Cbl-b inhibition. Commun Biol. 6, 1272
Passalacqua, L. F. M., Starich, M. R., Link, K. A., Wu, J., Knutson, J. R., Tjandra, N., Jaffrey, S. R., and Ferré-D'Amaré, A. R. (2023) Co-crystal structures of the fluorogenic aptamer Beetroot show that close homology may not predict similar RNA architecture. Nat Commun. 14, 2969
Teron, K. I. Negron, and Das, C. (2023) Cocrystallization of ubiquitin-deubiquitinase complexes through disulfide linkage. Acta Crystallogr D Struct Biol. 79, 1044-1055
Serganov, A., Huang, L., and Patel, D. J. (2009) Coenzyme recognition and gene regulation by a flavin mononucleotide riboswitch. Nature. 458, 233-7
Lynch, M. J., Levenson, R., Kim, E. A., Sircar, R., Blair, D. F., Dahlquist, F. W., and Crane, B. R. (2017) Co-Folding of a FliF-FliG Split Domain Forms the Basis of the MS:C Ring Interface within the Bacterial Flagellar Motor. Structure. 25, 317-328
Cui, H., M Ali, Y., Goyal, P., Zhang, K., Loh, J. Ying, Trybus, K. M., and Solmaz, S. R. (2020) Coiled-coil registry shifts in the F684I mutant of Bicaudal D result in cargo-independent activation of dynein motility. Traffic. 10.1111/tra.12734
Gunaratne, R., Kumar, S., Frederiksen, J. W., Stayrook, S., Lohrmann, J. L., Perry, K., Bompiani, K. M., Chabata, C. V., Thalji, N. K., Ho, M. D., Arepally, G., Camire, R. M., Krishnaswamy, S., and Sullenger, B. A. (2018) Combination of aptamer and drug for reversible anticoagulation in cardiopulmonary bypass. Nat Biotechnol. 10.1038/nbt.4153
Wang, Q., Michailidis, E., Yu, Y., Wang, Z., Hurley, A. M., Oren, D. A., Mayer, C. T., Gazumyan, A., Liu, Z., Zhou, Y., Schoofs, T., Yao, K. - H., Nieke, J. P., Wu, J., Jiang, Q., Zou, C., Kabbani, M., Quirk, C., Oliveira, T., Chhosphel, K., Zhang, Q., Schneider, W. M., Jahan, C., Ying, T., Horowitz, J., Caskey, M., Jankovic, M., Robbiani, D. F., Wen, Y., de Jong, Y. P., Rice, C. M., and Nussenzweig, M. C. (2020) A Combination of Human Broadly Neutralizing Antibodies against Hepatitis B Virus HBsAg with Distinct Epitopes Suppresses Escape Mutations. Cell Host Microbe. 28, 335-349.e6
Foster, B. M., Rosenberg, D., Salvo, H., Stephens, K. L., Bintz, B. J., Hammel, M., Ellenberger, T., Gainey, M. D., and Wallen, J. R. (2019) Combined Solution and Crystal Methods Reveal the Electrostatic Tethers That Provide a Flexible Platform for Replication Activities in the Bacteriophage T7 Replisome. Biochemistry. 58, 4466-4479
Simpson, B. W., Pahil, K. S., Owens, T. W., Lundstedt, E. A., Davis, R. M., Kahne, D., and Ruiz, N. (2019) Combining Mutations That Inhibit Two Distinct Steps of the ATP Hydrolysis Cycle Restores Wild-Type Function in the Lipopolysaccharide Transporter and Shows that ATP Binding Triggers Transport. MBio. 10.1128/mBio.01931-19
Dai, Q., Ren, A., Westholm, J. O., Duan, H., Patel, D. J., and Lai, E. C. (2015) Common and distinct DNA-binding and regulatory activities of the BEN-solo transcription factor family. Genes Dev. 29, 48-62
Whitley, M. J., Tran, T. H., Rigby, M., Yi, M., Dharmaiah, S., Waybright, T. J., Ramakrishnan, N., Perkins, S., Taylor, T., Messing, S., Esposito, D., Nissley, D. V., McCormick, F., Stephen, A. G., Turbyville, T., Cornilescu, G., and Simanshu, D. K. (2024) Comparative analysis of KRAS4a and KRAS4b splice variants reveals distinctive structural and functional properties. Sci Adv. 10, eadj4137
Harrison, S. A., Naretto, A., Balakrishnan, S., Perera, Y. R., and Chazin, W. J. (2023) Comparative analysis of the physical properties of murine and human S100A7: Insight into why zinc piracy is mediated by human but not murine S100A7. J Biol Chem. 299, 105292
Sukumar, N. (2014) A comparative analysis on X-ray structure of cobalamin binding proteins. 23rd International Union of Crystallography (IuCr) and General Assembly, August 5–12, 2014
Miallau, L., Jain, P., Arbing, M. A., Cascio, D., Phan, T., Ahn, C. J., Chan, S., Chernishof, I., Maxson, M., Chiang, J., Jacobs, W. R., and Eisenberg, D. S. (2013) Comparative proteomics identifies the cell-associated lethality of M. tuberculosis RelBE-like toxin-antitoxin complexes. Structure. 21, 627-37
Hudson, J. D., Tamilselvan, E., Sotomayor, M., and Cooper, S. R. (2021) A complete Protocadherin-19 ectodomain model for evaluating epilepsy-causing mutations and potential protein interaction sites. Structure. 29, 1128-1143.e4
Morar, M., Anand, R., Hoskins, A. A., Stubbe, J. A., and Ealick, S. E. (2006) Complexed structures of formylglycinamide ribonucleotide amidotransferase from Thermotoga maritima describe a novel ATP binding protein superfamily. Biochemistry. 45, 14880-95
Bale, S., Baba, K., McCloskey, D. E., Pegg, A. E., and Ealick, S. E. (2010) Complexes of Thermotoga maritimaS-adenosylmethionine decarboxylase provide insights into substrate specificity. Acta Crystallogr D Biol Crystallogr. 66, 181-9

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