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McCarthy, K. R., Timpona, J. L., Jenni, S., Bloyet, L. - M., Brusic, V., Johnson, W. E., Whelan, S. P. J., and Robinson-McCarthy, L. R. (2020) Structure of the Receptor Binding Domain of EnvP(b)1, an Endogenous Retroviral Envelope Protein Expressed in Human Tissues. mBio. 10.1128/mBio.02772-20
Yin, F. Fang, Bailey, S., C Innis, A., Ciubotaru, M., Kamtekar, S., Steitz, T. A., and Schatz, D. G. (2009) Structure of the RAG1 nonamer binding domain with DNA reveals a dimer that mediates DNA synapsis. Nat Struct Mol Biol. 16, 499-508
Ardiccioni, C., Clarke, O. B., Tomasek, D., Issa, H. A., von Alpen, D. C., Pond, H. L., Banerjee, S., Rajashankar, K. R., Liu, Q., Guan, Z., Li, C., Kloss, B., Bruni, R., Kloppmann, E., Rost, B., M Manzini, C., Shapiro, L., and Mancia, F. (2016) Structure of the polyisoprenyl-phosphate glycosyltransferase GtrB and insights into the mechanism of catalysis. Nat Commun. 7, 10175
Ardiccioni, C., Clarke, O. B., Tomasek, D., Issa, H. A., von Alpen, D. C., Pond, H. L., Banerjee, S., Rajashankar, K. R., Liu, Q., Guan, Z., Li, C., Kloss, B., Bruni, R., Kloppmann, E., Rost, B., M Manzini, C., Shapiro, L., and Mancia, F. (2016) Structure of the polyisoprenyl-phosphate glycosyltransferase GtrB and insights into the mechanism of catalysis. Nat Commun. 7, 10175
McCulloch, K. M., Mukherjee, T., Begley, T. P., and Ealick, S. E. (2009) Structure of the PLP degradative enzyme 2-methyl-3-hydroxypyridine-5-carboxylic acid oxygenase from Mesorhizobium loti MAFF303099 and its mechanistic implications. Biochemistry. 48, 4139-49
Cabarca, S., de Souza, M. Frazão, de Oliveira, A. Albert, Muniz, G. S. Vignoli, M Lamy, T., Reis, C. Vinicius D., Takarada, J., Effer, B., Souza, L. Santos, de la Torre, L. Iriarte, Couñago, R., Oliveira, C. Luis Pinto, and Balan, A. (2021) Structure of the PknF and conformational changes induced in forkhead-associated regulatory domains. Curr Res Struct Biol. 3, 165-178
Gordon, W. R., Roy, M., Vardar-Ulu, D., Garfinkel, M., Mansour, M. R., Aster, J. C., and Blacklow, S. C. (2009) Structure of the Notch1-negative regulatory region: implications for normal activation and pathogenic signaling in T-ALL. Blood. 113, 4381-90
Mompeán, M., Li, W., Li, J., Laage, S., Siemer, A. B., Bozkurt, G., Wu, H., and McDermott, A. E. (2018) The Structure of the Necrosome RIPK1-RIPK3 Core, a Human Hetero-Amyloid Signaling Complex. Cell. 173, 1244-1253.e10
Brown, B. L., Kardon, J. R., Sauer, R. T., and Baker, T. A. (2018) Structure of the Mitochondrial Aminolevulinic Acid Synthase, a Key Heme Biosynthetic Enzyme. Structure. 10.1016/j.str.2018.02.012
Brown, B. L., Kardon, J. R., Sauer, R. T., and Baker, T. A. (2018) Structure of the Mitochondrial Aminolevulinic Acid Synthase, a Key Heme Biosynthetic Enzyme. Structure. 10.1016/j.str.2018.02.012
Bobik, T. A., Morales, E. J., Shin, A., Cascio, D., Sawaya, M. R., Arbing, M., Yeates, T. O., and Rasche, M. E. (2014) Structure of the methanofuran/methanopterin-biosynthetic enzyme MJ1099 from Methanocaldococcus jannaschii. Acta Crystallogr F Struct Biol Commun. 70, 1472-9
Chen, P., Lam, K. - H., Liu, Z., Mindlin, F. A., Chen, B., Gutierrez, C. B., Huang, L., Zhang, Y., Hamza, T., Feng, H., Matsui, T., Bowen, M. E., Perry, K., and Jin, R. (2019) Structure of the full-length Clostridium difficile toxin B. Nat Struct Mol Biol. 10.1038/s41594-019-0268-0
Joo, W., Xu, G., Persky, N. S., Smogorzewska, A., Rudge, D. G., Buzovetsky, O., Elledge, S. J., and Pavletich, N. P. (2011) Structure of the FANCI-FANCD2 complex: insights into the Fanconi anemia DNA repair pathway. Science. 333, 312-6
Lehmann, C., Begley, T. P., and Ealick, S. E. (2006) Structure of the Escherichia coli ThiS-ThiF complex, a key component of the sulfur transfer system in thiamin biosynthesis. Biochemistry. 45, 11-9
Bowman, B. R., Lee, S., Wang, S., and Verdine, G. L. (2008) Structure of the E. coli DNA glycosylase AlkA bound to the ends of duplex DNA: a system for the structure determination of lesion-containing DNA. Structure. 16, 1166-74
Bodnar, N. O., Kim, K. H., Ji, Z., Wales, T. E., Svetlov, V., Nudler, E., Engen, J. R., Walz, T., and Rapoport, T. A. (2018) Structure of the Cdc48 ATPase with its ubiquitin-binding cofactor Ufd1-Npl4. Nat Struct Mol Biol. 25, 616-622
Liu, Z., Frutos, S., Bick, M. J., Vila-Perelló, M., Debelouchina, G. T., Darst, S. A., and Muir, T. W. (2014) Structure of the branched intermediate in protein splicing. Proc Natl Acad Sci U S A. 111, 8422-7
Corbett, K. D., and Berger, J. M. (2010) Structure of the ATP-binding domain of Plasmodium falciparum Hsp90. Proteins. 78, 2738-44
Green, M. N., Gangwar, S. Pal, Michard, E., Simon, A. A., Portes, M. Teresa, Barbosa-Caro, J., Wudick, M. M., Lizzio, M. A., Klykov, O., Yelshanskaya, M. V., Feijó, J. A., and Sobolevsky, A. I. (2021) Structure of the Arabidopsis thaliana glutamate receptor-like channel GLR3.4. Mol Cell. 10.1016/j.molcel.2021.05.025
Ha, B. Hak, Simpson, M. Adam, Koleske, A. J., and Boggon, T. J. (2015) Structure of the ABL2/ARG kinase in complex with dasatinib. Acta Crystallogr F Struct Biol Commun. 71, 443-8
Reha-Krantz, L. J., Hariharan, C., Subuddhi, U., Xia, S., Zhao, C., Beckman, J., Christian, T., and Konigsberg, W. (2011) Structure of the 2-aminopurine-cytosine base pair formed in the polymerase active site of the RB69 Y567A-DNA polymerase. Biochemistry. 50, 10136-49
Basu, R., Eichhorn, C. D., Cheng, R., Peterson, R. D., and Feigon, J. (2020) Structure of telomerase protein Pof8 C-terminal domain is an xRRM conserved among LARP7 proteins. RNA Biol. 10.1080/15476286.2020.1836891
Bailey, S., Wing, R. A., and Steitz, T. A. (2006) The structure of T. aquaticus DNA polymerase III is distinct from eukaryotic replicative DNA polymerases. Cell. 126, 893-904
Ayres, C. A., Schormann, N., Senkovich, O., Fry, A., Banerjee, S., Ulett, G. C., and Chattopadhyay, D. (2014) Structure of Streptococcus agalactiae glyceraldehyde-3-phosphate dehydrogenase holoenzyme reveals a novel surface. Acta Crystallogr F Struct Biol Commun. 70, 1333-9
Blank, P. N., Shinsky, S. A., and Christianson, D. W. (2019) Structure of Sesquisabinene Synthase 1, a Terpenoid Cyclase That Generates a Strained [3.1.0] Bridged-Bicyclic Product. ACS Chem Biol. 10.1021/acschembio.9b00218

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