Publications

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Gordon, W. R., Vardar-Ulu, D., L'Heureux, S., Ashworth, T., Malecki, M. J., Sanchez-Irizarry, C., McArthur, D. G., Histen, G., Mitchell, J. L., Aster, J. C., and Blacklow, S. C. (2009) Effects of S1 cleavage on the structure, surface export, and signaling activity of human Notch1 and Notch2. PLoS One. 4, e6613
Goodman, K. M., Rubinstein, R., Dan, H., Bahna, F., Mannepalli, S., Ahlsen, G., Thu, C. Aye, Sampogna, R. V., Maniatis, T., Honig, B., and Shapiro, L. (2017) Protocadherin cis-dimer architecture and recognition unit diversity. Proc Natl Acad Sci U S A. 10.1073/pnas.1713449114
Goodman, K. M., Yamagata, M., Jin, X., Mannepalli, S., Katsamba, P. S., Ahlsen, G., Sergeeva, A. P., Honig, B., Sanes, J. R., and Shapiro, L. (2016) Molecular basis of sidekick-mediated cell-cell adhesion and specificity. Elife. 10.7554/eLife.19058
Goodman, K. Marie, Rubinstein, R., Thu, C. Aye, Mannepalli, S., Bahna, F., Ahlsen, G., Rittenhouse, C., Maniatis, T., Honig, B., and Shapiro, L. (2016) γ-Protocadherin structural diversity and functional implications.. Elife. 10.7554/eLife.20930
Goodman, K. Marie, Rubinstein, R., Thu, C. Aye, Bahna, F., Mannepalli, S., Ahlsen, G., Rittenhouse, C., Maniatis, T., Honig, B., and Shapiro, L. (2016) Structural Basis of Diverse Homophilic Recognition by Clustered α- and β-Protocadherins.. Neuron. 90, 709-23
Goodman, M. C., Xu, S., Rouzer, C. A., Banerjee, S., Ghebreselasie, K., Migliore, M., Piomelli, D., and Marnett, L. J. (2018) Dual cyclooxygenase-fatty acid amide hydrolase inhibitor exploits novel binding interactions in the cyclooxygenase active site. J Biol Chem. 10.1074/jbc.M117.802058
Goodman, K. Marie, Katsamba, P. S., Rubinstein, R., Ahlsen, G., Bahna, F., Mannepalli, S., Dan, H., Sampogna, R. V., Shapiro, L., and Honig, B. (2022) How clustered protocadherin binding specificity is tuned for neuronal self-/nonself-recognition. Elife. 10.7554/eLife.72416
Gonzalez, R., Soule, J., Phan, N., Wicht, D. K., and Dowling, D. P. (2024) Structural, biophysical, and biochemical insights into C-S bond cleavage by dimethylsulfone monooxygenase. Proc Natl Acad Sci U S A. 121, e2401858121
Gong, Z., Wang, W., Omari, K. El, Lebedev, A. A., Clarke, O. B., and Hendrickson, W. A. (2023) Crystal structure of LGR ligand α2/β5 from with implications for the evolution of glycoprotein hormones.. Proc Natl Acad Sci U S A. 120, e2218630120
Goldman, P. J., Ryan, K. S., Hamill, M. J., Howard-Jones, A. R., Walsh, C. T., Elliott, S. J., and Drennan, C. L. (2012) An unusual role for a mobile flavin in StaC-like indolocarbazole biosynthetic enzymes. Chem Biol. 19, 855-65
Goldman, P. J., Grove, T. L., Sites, L. A., McLaughlin, M. I., Booker, S. J., and Drennan, C. L. (2013) X-ray structure of an AdoMet radical activase reveals an anaerobic solution for formylglycine posttranslational modification. Proc Natl Acad Sci U S A. 110, 8519-24
Goldman, P. J., Grove, T. L., Booker, S. J., and Drennan, C. L. (2013) X-ray analysis of butirosin biosynthetic enzyme BtrN redefines structural motifs for AdoMet radical chemistry. Proc Natl Acad Sci U S A. 110, 15949-54
Goldgur, Y., Susi, P., Karelehto, E., Sanmark, H., Lamminmäki, U., Oricchio, E., Wendel, H. - G., Nikolov, D. B., and Himanen, J. P. (2014) Generation and characterization of a single-chain anti-EphA2 antibody. Growth Factors. 32, 214-22
Golden, B. L., Kim, H., and Chase, E. (2005) Crystal structure of a phage Twort group I ribozyme-product complex. Nat Struct Mol Biol. 12, 82-9
Golczak, M., Kiser, P. D., Sears, A. E., Lodowski, D. T., Blaner, W. S., and Palczewski, K. (2012) Structural basis for the acyltransferase activity of lecithin:retinol acyltransferase-like proteins. J Biol Chem. 287, 23790-807
Golczak, M., Sears, A. E., Kiser, P. D., and Palczewski, K. (2015) LRAT-specific domain facilitates vitamin A metabolism by domain swapping in HRASLS3. Nat Chem Biol. 11, 26-32
Golani, L. K., Wallace-Povirk, A., Deis, S. M., Wong, J., Ke, J., Gu, X., Raghavan, S., Wilson, M. R., Li, X., Polin, L., de Waal, P. W., White, K., Kushner, J., O'Connor, C., Hou, Z., H Xu, E., Melcher, K., Dann, C. E., Matherly, L. H., and Gangjee, A. (2016) Tumor Targeting with Novel 6-Substituted Pyrrolo [2,3-d] Pyrimidine Antifolates with Heteroatom Bridge Substitutions via Cellular Uptake by Folate Receptor α and the Proton-Coupled Folate Transporter and Inhibition of de Novo Purine Nucleotide Biosynthes. J Med Chem. 59, 7856-76
Gnann, A. D., Xia, Y., Soule, J., Barthélemy, C., Mawani, J. S., Musoke, S. Nzikoba, Castellano, B. M., Brignole, E. J., Frueh, D. P., and Dowling, D. P. (2022) High-resolution structures of a siderophore-producing cyclization domain from Yersinia pestis offer a refined proposal of substrate binding. J Biol Chem. 298, 102454
Gleason, J. E., Galaleldeen, A., Peterson, R. L., Taylor, A. B., Holloway, S. P., Waninger-Saroni, J., Cormack, B. P., Cabelli, D. E., P Hart, J., and Culotta, V. Cizewski (2014) Candida albicans SOD5 represents the prototype of an unprecedented class of Cu-only superoxide dismutases required for pathogen defense. Proc Natl Acad Sci U S A. 111, 5866-71
Gkeka, A., Aresta-Branco, F., Triller, G., Vlachou, E. P., van Straaten, M., Lilic, M., Olinares, P. Dominic B., Perez, K., Chait, B. T., Blatnik, R., Ruppert, T., Verdi, J. P., C Stebbins, E., and F Papavasiliou, N. (2023) Immunodominant surface epitopes power immune evasion in the African trypanosome. Cell Rep. 42, 112262
Gitlin, A. D., Maltzman, A., Kanno, Y., Heger, K., Reja, R., Schubert, A. F., Wierciszewski, L. J., Pantua, H., Kapadia, S. B., Harris, S. F., Webster, J. D., Newton, K., and Dixit, V. M. (2024) N4BP1 coordinates ubiquitin-dependent crosstalk within the IκB kinase family to limit Toll-like receptor signaling and inflammation.. Immunity. 57, 973-986.e7
Girish, T. S., McGinty, R. K., and Tan, S. (2016) Multivalent Interactions by the Set8 Histone Methyltransferase With Its Nucleosome Substrate. J Mol Biol. 428, 1531-43
Ginn, J., Jiang, X., Sun, S., Michino, M., Huggins, D. J., Mbambo, Z., Jansen, R., Rhee, K. Y., Arango, N., Lima, C. D., Liverton, N., Imaeda, T., Okamoto, R., Kuroita, T., Aso, K., Stamford, A., Foley, M., Meinke, P. T., Nathan, C., and Bryk, R. (2021) Whole Cell Active Inhibitors of Mycobacterial Lipoamide Dehydrogenase Afford Selectivity over the Human Enzyme through Tight Binding Interactions. ACS Infect Dis. 7, 435-444
Gilleran, J. A., Ashraf, K., Delvillar, M., Eck, T., Fondekar, R., Miller, E. B., Hutchinson, A., Dong, A., Seitova, A., De Souza, M. Laureano, Augeri, D., Halabelian, L., Siekierka, J., Rotella, D. P., Gordon, J., Childers, W. E., Grier, M. C., Staker, B. L., Roberge, J. Y., and Bhanot, P. (2024) Structure-Activity Relationship of a Pyrrole Based Series of PfPKG Inhibitors as Anti-Malarials. J Med Chem. 67, 3467-3503
Gilbert, N. C., Neau, D. B., and Newcomer, M. E. (2018) Expression of an 8R-Lipoxygenase From the Coral Plexaura homomalla. Methods Enzymol. 605, 33-49

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