Publications

Found 116 results
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A
Ahmad, M. Faiz, Huff, S. E., Pink, J., Alam, I., Zhang, A., Perry, K., Harris, M. E., Misko, T., Porwal, S. K., Oleinick, N. L., Miyagi, M., Viswanathan, R., and Dealwis, C. Godfrey (2015) Identification of Non-nucleoside Human Ribonucleotide Reductase Modulators. J Med Chem. 58, 9498-509
Ahmad, S., Wang, B., Walker, M. D., Tran, H. - K. R., Stogios, P. J., Savchenko, A., Grant, R. A., McArthur, A. G., Laub, M. T., and Whitney, J. C. (2019) An interbacterial toxin inhibits target cell growth by synthesizing (p)ppApp. Nature. 575, 674-678
Ahmed, M., Goldgur, Y., Hu, J., Guo, H. - F., and Cheung, N. - K. V. (2013) In silico driven redesign of a clinically relevant antibody for the treatment of GD2 positive tumors. PLoS One. 8, e63359
Andersen, K. Røjkjær (2017) Insights into Rad3 kinase recruitment from the crystal structure of the DNA damage checkpoint protein Rad26. J Biol Chem. 292, 8149-8157
Araghi, R. Rezaei, Bird, G. H., Ryan, J. A., Jenson, J. M., Godes, M., Pritz, J. R., Grant, R. A., Letai, A., Walensky, L. D., and Keating, A. E. (2018) Iterative optimization yields Mcl-1-targeting stapled peptides with selective cytotoxicity to Mcl-1-dependent cancer cells. Proc Natl Acad Sci U S A. 115, E886-E895
Ausin, I., Greenberg, M. V. C., Simanshu, D. K., Hale, C. J., Vashisht, A. A., Simon, S. A., Lee, T. -fen, Feng, S., Española, S. D., Meyers, B. C., Wohlschlegel, J. A., Patel, D. J., and Jacobsen, S. E. (2012) INVOLVED IN DE NOVO 2-containing complex involved in RNA-directed DNA methylation in Arabidopsis. Proc Natl Acad Sci U S A. 109, 8374-81
B
Bajic, G., Maron, M. J., Adachi, Y., Onodera, T., McCarthy, K. R., McGee, C. E., Sempowski, G. D., Takahashi, Y., Kelsoe, G., Kuraoka, M., and Schmidt, A. G. (2019) Influenza Antigen Engineering Focuses Immune Responses to a Subdominant but Broadly Protective Viral Epitope. Cell Host Microbe. 25, 827-835.e6
Balaratnam, S., Torrey, Z. R., Calabrese, D. R., Banco, M. T., Yazdani, K., Liang, X., Fullenkamp, C. R., Seshadri, S., Holewinski, R. J., Andresson, T., Ferré-D'Amaré, A. R., Incarnato, D., and Schneekloth, J. S. (2023) Investigating the NRAS 5' UTR as a target for small molecules. Cell Chem Biol. 30, 643-657.e8
Ben-Nun, Y., Seo, H. - S., Harvey, E. P., Hauseman, Z. J., Wales, T. E., Newman, C. E., Cathcart, A. M., Engen, J. R., Dhe-Paganon, S., and Walensky, L. D. (2020) Identification of a Structural Determinant for Selective Targeting of HDMX. Structure. 28, 847-857.e5
Bhardwaj, R., Lindinger, S., Neuberger, A., Nadezhdin, K. D., Singh, A. K., Cunha, M. R., Derler, I., Gyimesi, G., Reymond, J. - L., Hediger, M. A., Romanin, C., and Sobolevsky, A. I. (2020) Inactivation-mimicking block of the epithelial calcium channel TRPV6. Sci Adv. 10.1126/sciadv.abe1508
Bhattacharjee, D., Bakar, J., Chitnis, S. P., Sausville, E. L., Ashtekar, K. Dilip, Mendelson, B. E., Long, K., Smith, J. C., Heppner, D. E., and Sheltzer, J. M. (2023) Inhibition of a lower potency target drives the anticancer activity of a clinical p38 inhibitor. Cell Chem Biol. 30, 1211-1222.e5
Brumshtein, B., Esswein, S. R., Sawaya, M. R., Rosenberg, G., Ly, A. T., Landau, M., and Eisenberg, D. S. (2018) Identification of two principal amyloid-driving segments in variable domains of Ig light chains in systemic light chain amyloidosis. J Biol Chem. 10.1074/jbc.RA118.004142
Brumshtein, B., Esswein, S. R., Salwinski, L., Phillips, M. L., Ly, A. T., Cascio, D., Sawaya, M. R., and Eisenberg, D. S. (2015) Inhibition by small-molecule ligands of formation of amyloid fibrils of an immunoglobulin light chain variable domain. Elife. 4, e10935
Bubenik, M., Mader, P., Mochirian, P., Vallée, F., Clark, J., Truchon, J. - F., Perryman, A. L., Pau, V., Kurinov, I., Zahn, K. E., Leclaire, M. - E., Papp, R., Mathieu, M. - C., Hamel, M., Duffy, N. M., Godbout, C., Casas-Selves, M., Falgueyret, J. - P., Baruah, P. S., Nicolas, O., Stocco, R., Poirier, H., Martino, G., Fortin, A. Bonneau, Roulston, A., Chefson, A., Dorich, S., St-Onge, M., Patel, P., Pellerin, C., Ciblat, S., Pinter, T., Barabé, F., Bakkouri, M. El, Parikh, P., Gervais, C., Sfeir, A., Mamane, Y., Morris, S. J., W Black, C., Sicheri, F., and Gallant, M. (2022) Identification of , an Orally Bioavailable Compound that Inhibits the DNA Polymerase Activity of Polθ.. J Med Chem. 10.1021/acs.jmedchem.2c00998
C
Cao, Q., Shin, W. Shik, Chan, H., Vuong, C. K., Dubois, B., Li, B., Murray, K. A., Sawaya, M. R., Feigon, J., Black, D. L., Eisenberg, D. S., and Jiang, L. (2018) Inhibiting amyloid-β cytotoxicity through its interaction with the cell surface receptor LilrB2 by structure-based design.. Nat Chem. 10.1038/s41557-018-0147-z
Chandran, S. S., Ma, J., Klatt, M. G., Dündar, F., Bandlamudi, C., Razavi, P., Wen, H. Y., Weigelt, B., Zumbo, P., Fu, S. Ning, Banks, L. B., Yi, F., Vercher, E., Etxeberria, I., Bestman, W. D., Paula, A. Da Cruz, Aricescu, I. S., Drilon, A., Betel, D., Scheinberg, D. A., Baker, B. M., and Klebanoff, C. A. (2022) Immunogenicity and therapeutic targeting of a public neoantigen derived from mutated PIK3CA. Nat Med. 28, 946-957
Chen, Y., Farquhar, E. R., Chance, M. R., Palczewski, K., and Kiser, P. D. (2012) Insights into substrate specificity and metal activation of mammalian tetrahedral aspartyl aminopeptidase. J Biol Chem. 287, 13356-70
Chen, C., Ha, B. Hak, Thévenin, A. F., Lou, H. Jane, Zhang, R., Yip, K. Y., Peterson, J. R., Gerstein, M., Kim, P. M., Filippakopoulos, P., Knapp, S., Boggon, T. J., and Turk, B. E. (2014) Identification of a major determinant for serine-threonine kinase phosphoacceptor specificity. Mol Cell. 53, 140-7
Choi, E. H., Suh, S., Sander, C. L., Hernandez, C. J. Ortiz, Bulman, E. R., Khadka, N., Dong, Z., Shi, W., Palczewski, K., and Kiser, P. D. (2018) Insights into the pathogenesis of dominant retinitis pigmentosa associated with a D477G mutation in RPE65. Hum Mol Genet. 10.1093/hmg/ddy128
D
Dang, B., Shen, R., Kubota, T., Mandal, K., Bezanilla, F., Roux, B., and Kent, S. B. H. (2017) Inversion of the Side-Chain Stereochemistry of Indvidual Thr or Ile Residues in a Protein Molecule: Impact on the Folding, Stability, and Structure of the ShK Toxin. Angew Chem Int Ed Engl. 56, 3324-3328
Deinema, M. S., Perry, K., Kearns, S. P., D’Antonio, E. L., and D’Antonio, J. (2014) Inhibition of Trypanosoma cruzi Glucokinase with 2,6-Dideoxy-2,6-Diamino-D-Glucose. 66th Southeastern Regional Meeting of the American Chemical Society, October 16-19, 2014
Dhatwalia, R., Singh, H., Solano, L. M., Oppenheimer, M., Robinson, R. M., Ellerbrock, J. F., Sobrado, P., and Tanner, J. J. (2012) Identification of the NAD(P)H binding site of eukaryotic UDP-galactopyranose mutase. J Am Chem Soc. 134, 18132-8
Di Costanzo, L., Ilies, M., Thorn, K. J., and Christianson, D. W. (2010) Inhibition of human arginase I by substrate and product analogues. Arch Biochem Biophys. 496, 101-8
Dong, G., Wearsch, P. A., Peaper, D. R., Cresswell, P., and Reinisch, K. M. (2009) Insights into MHC class I peptide loading from the structure of the tapasin-ERp57 thiol oxidoreductase heterodimer. Immunity. 30, 21-32
E
Eiler, D., Lin, J., Simonetti, A., Klaholz, B. P., and Steitz, T. A. (2013) Initiation factor 2 crystal structure reveals a different domain organization from eukaryotic initiation factor 5B and mechanism among translational GTPases. Proc Natl Acad Sci U S A. 110, 15662-7

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