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2023

Chen, W. - H., Hajduczki, A., Martinez, E. J., Bai, H., Matz, H., Hill, T. M., Lewitus, E., Chang, W. C., Dawit, L., Peterson, C. E., Rees, P. A., Ajayi, A. B., Golub, E. S., Swafford, I., Dussupt, V., David, S., Mayer, S. V., Soman, S., Kuklis, C., Corbitt, C., King, J., Choe, M., Sankhala, R. S., Thomas, P. V., Zemil, M., Wieczorek, L., Hart, T., Duso, D., Kummer, L., Yan, L., Sterling, S. L., Laing, E. D., Broder, C. C., Williams, J. K., Davidson, E., Doranz, B. J., Krebs, S. J., Polonis, V. R., Paquin-Proulx, D., Rolland, M., Reiley, W. W., Gromowski, G. D., Modjarrad, K., Dooley, H., and M Joyce, G. (2023) Shark nanobodies with potent SARS-CoV-2 neutralizing activity and broad sarbecovirus reactivity. Nat Commun. 14, 580

Chen, W. - H., Hajduczki, A., Martinez, E. J., Bai, H., Matz, H., Hill, T. M., Lewitus, E., Chang, W. C., Dawit, L., Peterson, C. E., Rees, P. A., Ajayi, A. B., Golub, E. S., Swafford, I., Dussupt, V., David, S., Mayer, S. V., Soman, S., Kuklis, C., Corbitt, C., King, J., Choe, M., Sankhala, R. S., Thomas, P. V., Zemil, M., Wieczorek, L., Hart, T., Duso, D., Kummer, L., Yan, L., Sterling, S. L., Laing, E. D., Broder, C. C., Williams, J. K., Davidson, E., Doranz, B. J., Krebs, S. J., Polonis, V. R., Paquin-Proulx, D., Rolland, M., Reiley, W. W., Gromowski, G. D., Modjarrad, K., Dooley, H., and M Joyce, G. (2023) Shark nanobodies with potent SARS-CoV-2 neutralizing activity and broad sarbecovirus reactivity. Nat Commun. 14, 580

Chen, W. - H., Hajduczki, A., Martinez, E. J., Bai, H., Matz, H., Hill, T. M., Lewitus, E., Chang, W. C., Dawit, L., Peterson, C. E., Rees, P. A., Ajayi, A. B., Golub, E. S., Swafford, I., Dussupt, V., David, S., Mayer, S. V., Soman, S., Kuklis, C., Corbitt, C., King, J., Choe, M., Sankhala, R. S., Thomas, P. V., Zemil, M., Wieczorek, L., Hart, T., Duso, D., Kummer, L., Yan, L., Sterling, S. L., Laing, E. D., Broder, C. C., Williams, J. K., Davidson, E., Doranz, B. J., Krebs, S. J., Polonis, V. R., Paquin-Proulx, D., Rolland, M., Reiley, W. W., Gromowski, G. D., Modjarrad, K., Dooley, H., and M Joyce, G. (2023) Shark nanobodies with potent SARS-CoV-2 neutralizing activity and broad sarbecovirus reactivity. Nat Commun. 14, 580

Maiti, A., Buffalo, C. Z., Saurabh, S., Montecinos-Franjola, F., Hachey, J. S., Conlon, W. J., Tran, G. N., Hassan, B., Walters, K. J., Drobizhev, M., Moerner, W. E., Ghosh, P., Matsuo, H., Tsien, R. Y., Lin, J. Y., and Rodriguez, E. A. (2023) Structural and photophysical characterization of the small ultra-red fluorescent protein. Nat Commun. 14, 4155

Liu, Z., Lee, P. - G., Krez, N., Lam, K. - H., Liu, H., Przykopanski, A., Chen, P., Yao, G., Zhang, S., Tremblay, J. M., Perry, K., Shoemaker, C. B., Rummel, A., Dong, M., and Jin, R. (2023) Structural basis for botulinum neurotoxin E recognition of synaptic vesicle protein 2. Nat Commun. 14, 2338

Nguyen, H. An, Hoffer, E. D., Fagan, C. E., Maehigashi, T., and Dunham, C. M. (2023) Structural basis for reduced ribosomal A-site fidelity in response to P-site codon-anticodon mismatches. J Biol Chem. 299, 104608

Nguyen, H. An, Hoffer, E. D., Fagan, C. E., Maehigashi, T., and Dunham, C. M. (2023) Structural basis for reduced ribosomal A-site fidelity in response to P-site codon-anticodon mismatches. bioRxiv. 10.1101/2023.01.28.526049

Rudolph, M. J., Davis, S. A., Haque, H. M. Emranul, Weis, D. D., Vance, D. J., Piazza, C. Lyn, Ejemel, M., Cavacini, L., Wang, Y., M Mbow, L., Gilmore, R. D., and Mantis, N. J. (2023) Structural Elucidation of a Protective B Cell Epitope on Outer Surface Protein C (OspC) of the Lyme Disease Spirochete, Borreliella burgdorferi. mBio. 10.1128/mbio.02981-22

Chen, C. - W., Leimer, N., Syroegin, E. A., Dunand, C., Bulman, Z. P., Lewis, K., Polikanov, Y. S., and Svetlov, M. S. (2023) Structural insights into the mechanism of overcoming Erm-mediated resistance by macrolides acting together with hygromycin-A. Nat Commun. 14, 4196

Tkacik, E., Li, K., Del Pino, G. Gonzalez-, Ha, B. Hak, Vinals, J., Park, E., Beyett, T. S., and Eck, M. J. (2023) Structure and RAF family kinase isoform selectivity of type II RAF inhibitors tovorafenib and naporafenib. J Biol Chem. 299, 104634

Rudolph, M. J., Davis, S. A., Haque, H. M. Emranul, Ejemel, M., Cavacini, L. A., Vance, D. J., Willsey, G. G., Piazza, C. Lyn, Weis, D. D., Wang, Y., and Mantis, N. J. (2023) Structure of a transmission blocking antibody in complex with Outer surface protein A from the Lyme disease spirochete, Borreliella burgdorferi. Proteins. 10.1002/prot.26549

Vaccaro, F. A., Born, D. A., and Drennan, C. L. (2023) Structure of metallochaperone in complex with the cobalamin-binding domain of its target mutase provides insight into cofactor delivery. Proc Natl Acad Sci U S A. 120, e2214085120

Grasty, K. C., Guzik, C., D'Lauro, E. J., Padrick, S. B., Beld, J., and Loll, P. J. (2023) Structure of VanS from vancomycin-resistant enterococci: A sensor kinase with weak ATP binding.. J Biol Chem. 299, 103001

Jensen, J. L., Sankhala, R. S., Dussupt, V., Bai, H., Hajduczki, A., Lal, K. G., Chang, W. C., Martinez, E. J., Peterson, C. E., Golub, E. S., Rees, P. A., Mendez-Rivera, L., Zemil, M., Kavusak, E., Mayer, S. V., Wieczorek, L., Kannan, S., Doranz, B. J., Davidson, E., Yang, E. Sung, Zhang, Y., Chen, M., Choe, M., Wang, L., Gromowski, G. D., Koup, R. A., Michael, N. L., Polonis, V. R., Rolland, M., Modjarrad, K., Krebs, S. J., and M Joyce, G. (2023) Targeting the Spike Receptor Binding Domain Class V Cryptic Epitope by an Antibody with Pan-Sarbecovirus Activity. J Virol. 97, e0159622

Jensen, J. L., Sankhala, R. S., Dussupt, V., Bai, H., Hajduczki, A., Lal, K. G., Chang, W. C., Martinez, E. J., Peterson, C. E., Golub, E. S., Rees, P. A., Mendez-Rivera, L., Zemil, M., Kavusak, E., Mayer, S. V., Wieczorek, L., Kannan, S., Doranz, B. J., Davidson, E., Yang, E. Sung, Zhang, Y., Chen, M., Choe, M., Wang, L., Gromowski, G. D., Koup, R. A., Michael, N. L., Polonis, V. R., Rolland, M., Modjarrad, K., Krebs, S. J., and M Joyce, G. (2023) Targeting the Spike Receptor Binding Domain Class V Cryptic Epitope by an Antibody with Pan-Sarbecovirus Activity. J Virol. 97, e0159622

Jensen, J. L., Sankhala, R. S., Dussupt, V., Bai, H., Hajduczki, A., Lal, K. G., Chang, W. C., Martinez, E. J., Peterson, C. E., Golub, E. S., Rees, P. A., Mendez-Rivera, L., Zemil, M., Kavusak, E., Mayer, S. V., Wieczorek, L., Kannan, S., Doranz, B. J., Davidson, E., Yang, E. Sung, Zhang, Y., Chen, M., Choe, M., Wang, L., Gromowski, G. D., Koup, R. A., Michael, N. L., Polonis, V. R., Rolland, M., Modjarrad, K., Krebs, S. J., and M Joyce, G. (2023) Targeting the Spike Receptor Binding Domain Class V Cryptic Epitope by an Antibody with Pan-Sarbecovirus Activity. J Virol. 97, e0159622

Morgado-Palacin, L., Brown, J. A., Martinez, T. F., Garcia-Pedrero, J. M., Forouhar, F., S Quinn, A., Reglero, C., Vaughan, J., Heydary, Y. Hajy, Donaldson, C., Rodriguez-Perales, S., Allonca, E., Granda-Diaz, R., Fernandez, A. F., Fraga, M. F., Kim, A. L., Santos-Juanes, J., Owens, D. M., Rodrigo, J. P., Saghatelian, A., and Ferrando, A. A. (2023) The TINCR ubiquitin-like microprotein is a tumor suppressor in squamous cell carcinoma. Nat Commun. 14, 1328

Zhao, S., Lu, J., Pan, B., Fan, H., Byrum, S. D., Xu, C., Kim, A., Guo, Y., Kanchi, K. L., Gong, W., Sun, T., Storey, A. J., Burkholder, N. T., Mackintosh, S. G., Kuhlers, P. C., Edmondson, R. D., Strahl, B. D., Diao, Y., Tackett, A. J., Raab, J. R., Cai, L., Song, J., and Wang, G. Greg (2023) TNRC18 engages H3K9me3 to mediate silencing of endogenous retrotransposons. Nature. 623, 633-642

Larson, G., Windsor, P., Smithwick, E., Shi, K., Aihara, H., Damodaran, A. Rama, and Bhagi-Damodaran, A. (2023) Understanding ATP binding to DosS catalytic domain with a short ATP-lid. bioRxiv. 10.1101/2023.05.29.542785

Larson, G. W., Windsor, P. K., Smithwick, E., Shi, K., Aihara, H., Damodaran, A. Rama, and Bhagi-Damodaran, A. (2023) Understanding ATP Binding to DosS Catalytic Domain with a Short ATP-Lid. Biochemistry. 62, 3283-3292

Sankhala, R. S., Dussupt, V., Donofrio, G., Gromowski, G. D., De La Barrera, R. A., Larocca, R. A., Mendez-Rivera, L., Lee, A., Choe, M., Zaky, W., Mantus, G., Jensen, J. L., Chen, W. - H., Gohain, N., Bai, H., McCracken, M. K., Mason, R. D., Leggat, D., Slike, B. M., Tran, U., Jian, N., Abbink, P., Peterson, R., Mendes, E. Araujo, Franca, R. Freitas de, Calvet, G. Amaral, de Filippis, A. Maria Bisp, McDermott, A., Roederer, M., Hernandez, M., Albertus, A., Davidson, E., Doranz, B. J., Rolland, M., Robb, M. L., Lynch, R. M., Barouch, D. H., Jarman, R. G., Thomas, S. J., Modjarrad, K., Michael, N. L., Krebs, S. J., and M Joyce, G. (2023) Zika-specific neutralizing antibodies targeting inter-dimer envelope epitopes. Cell Rep. 42, 112942

Sankhala, R. S., Dussupt, V., Donofrio, G., Gromowski, G. D., De La Barrera, R. A., Larocca, R. A., Mendez-Rivera, L., Lee, A., Choe, M., Zaky, W., Mantus, G., Jensen, J. L., Chen, W. - H., Gohain, N., Bai, H., McCracken, M. K., Mason, R. D., Leggat, D., Slike, B. M., Tran, U., Jian, N., Abbink, P., Peterson, R., Mendes, E. Araujo, Franca, R. Freitas de, Calvet, G. Amaral, de Filippis, A. Maria Bisp, McDermott, A., Roederer, M., Hernandez, M., Albertus, A., Davidson, E., Doranz, B. J., Rolland, M., Robb, M. L., Lynch, R. M., Barouch, D. H., Jarman, R. G., Thomas, S. J., Modjarrad, K., Michael, N. L., Krebs, S. J., and M Joyce, G. (2023) Zika-specific neutralizing antibodies targeting inter-dimer envelope epitopes. Cell Rep. 42, 112942

Sankhala, R. S., Dussupt, V., Donofrio, G., Gromowski, G. D., De La Barrera, R. A., Larocca, R. A., Mendez-Rivera, L., Lee, A., Choe, M., Zaky, W., Mantus, G., Jensen, J. L., Chen, W. - H., Gohain, N., Bai, H., McCracken, M. K., Mason, R. D., Leggat, D., Slike, B. M., Tran, U., Jian, N., Abbink, P., Peterson, R., Mendes, E. Araujo, Franca, R. Freitas de, Calvet, G. Amaral, de Filippis, A. Maria Bisp, McDermott, A., Roederer, M., Hernandez, M., Albertus, A., Davidson, E., Doranz, B. J., Rolland, M., Robb, M. L., Lynch, R. M., Barouch, D. H., Jarman, R. G., Thomas, S. J., Modjarrad, K., Michael, N. L., Krebs, S. J., and M Joyce, G. (2023) Zika-specific neutralizing antibodies targeting inter-dimer envelope epitopes. Cell Rep. 42, 112942

Sankhala, R. S., Dussupt, V., Donofrio, G., Gromowski, G. D., De La Barrera, R. A., Larocca, R. A., Mendez-Rivera, L., Lee, A., Choe, M., Zaky, W., Mantus, G., Jensen, J. L., Chen, W. - H., Gohain, N., Bai, H., McCracken, M. K., Mason, R. D., Leggat, D., Slike, B. M., Tran, U., Jian, N., Abbink, P., Peterson, R., Mendes, E. Araujo, Franca, R. Freitas de, Calvet, G. Amaral, de Filippis, A. Maria Bisp, McDermott, A., Roederer, M., Hernandez, M., Albertus, A., Davidson, E., Doranz, B. J., Rolland, M., Robb, M. L., Lynch, R. M., Barouch, D. H., Jarman, R. G., Thomas, S. J., Modjarrad, K., Michael, N. L., Krebs, S. J., and M Joyce, G. (2023) Zika-specific neutralizing antibodies targeting inter-dimer envelope epitopes. Cell Rep. 42, 112942

Sankhala, R. S., Dussupt, V., Donofrio, G., Gromowski, G. D., De La Barrera, R. A., Larocca, R. A., Mendez-Rivera, L., Lee, A., Choe, M., Zaky, W., Mantus, G., Jensen, J. L., Chen, W. - H., Gohain, N., Bai, H., McCracken, M. K., Mason, R. D., Leggat, D., Slike, B. M., Tran, U., Jian, N., Abbink, P., Peterson, R., Mendes, E. Araujo, Franca, R. Freitas de, Calvet, G. Amaral, de Filippis, A. Maria Bisp, McDermott, A., Roederer, M., Hernandez, M., Albertus, A., Davidson, E., Doranz, B. J., Rolland, M., Robb, M. L., Lynch, R. M., Barouch, D. H., Jarman, R. G., Thomas, S. J., Modjarrad, K., Michael, N. L., Krebs, S. J., and M Joyce, G. (2023) Zika-specific neutralizing antibodies targeting inter-dimer envelope epitopes. Cell Rep. 42, 112942

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The Northeastern Collaborative Access Team (NE-CAT) facility at the Advanced Photon Source at Argonne National Laboratory is managed by Cornell University and consists of eight member institutions:

Columbia University
Cornell University
Genentech
Harvard University
Memorial Sloan-Kettering Cancer Center
Massachusetts Institute of Technology
Rockefeller University
Yale University

Primary funding for this project comes from the National Institute of General Medical Sciences (NIGMS), a division of the National Institutes of Health (NIH). Additional financial support for NE-CAT comes from the member institutions.