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2021

Tayeb-Fligelman, E., Cheng, X., Tai, C., Bowler, J. T., Griner, S., Sawaya, M. R., Seidler, P. M., Jiang, Y. Xiao, Lu, J., Rosenberg, G. M., Salwinski, L., Abskharon, R., Zee, C. - T., Hou, K., Li, Y., Boyer, D. R., Murray, K. A., Falcon, G., Anderson, D. H., Cascio, D., Saelices, L., Damoiseaux, R., Guo, F., and Eisenberg, D. S. (2021) Inhibition of amyloid formation of the Nucleoprotein of SARS-CoV-2. bioRxiv. 10.1101/2021.03.05.434000

Tayeb-Fligelman, E., Cheng, X., Tai, C., Bowler, J. T., Griner, S., Sawaya, M. R., Seidler, P. M., Jiang, Y. Xiao, Lu, J., Rosenberg, G. M., Salwinski, L., Abskharon, R., Zee, C. - T., Hou, K., Li, Y., Boyer, D. R., Murray, K. A., Falcon, G., Anderson, D. H., Cascio, D., Saelices, L., Damoiseaux, R., Guo, F., and Eisenberg, D. S. (2021) Inhibition of amyloid formation of the Nucleoprotein of SARS-CoV-2. bioRxiv. 10.1101/2021.03.05.434000

Tran, T. H., Chan, A. H., Young, L. C., Bindu, L., Neale, C., Messing, S., Dharmaiah, S., Taylor, T., Denson, J. - P., Esposito, D., Nissley, D. V., Stephen, A. G., McCormick, F., and Simanshu, D. K. (2021) KRAS interaction with RAF1 RAS-binding domain and cysteine-rich domain provides insights into RAS-mediated RAF activation. Nat Commun. 12, 1176

Dussupt, V., Sankhala, R. S., Mendez-Rivera, L., Townsley, S. M., Schmidt, F., Wieczorek, L., Lal, K. G., Donofrio, G. C., Tran, U., Jackson, N. D., Zaky, W. I., Zemil, M., Tritsch, S. R., Chen, W. - H., Martinez, E. J., Ahmed, A., Choe, M., Chang, W. C., Hajduczki, A., Jian, N., Peterson, C. E., Rees, P. A., Rutkowska, M., Slike, B. M., Selverian, C. N., Swafford, I., Teng, I. - T., Thomas, P. V., Zhou, T., Smith, C. J., Currier, J. R., Kwong, P. D., Rolland, M., Davidson, E., Doranz, B. J., Mores, C. N., Hatziioannou, T., Reiley, W. W., Bieniasz, P. D., Paquin-Proulx, D., Gromowski, G. D., Polonis, V. R., Michael, N. L., Modjarrad, K., M Joyce, G., and Krebs, S. J. (2021) Low-dose in vivo protection and neutralization across SARS-CoV-2 variants by monoclonal antibody combinations. Nat Immunol. 10.1038/s41590-021-01068-z

Banerjee, S. (2021) The Mathematical Lens - Fourier Transform. University of Burdwan

Ubah, O. C., Lake, E. W., Gunaratne, G. S., Gallant, J. P., Fernie, M., Robertson, A. J., Marchant, J. S., Bold, T. D., Langlois, R. A., Matchett, W. E., Thiede, J. M., Shi, K., Yin, L., Moeller, N. H., Banerjee, S., Ferguson, L., Kovaleva, M., Porter, A. J., Aihara, H., LeBeau, A. M., and Barelle, C. J. (2021) Mechanisms of SARS-CoV-2 neutralization by shark variable new antigen receptors elucidated through X-ray crystallography. Nat Commun. 12, 7325

Ubah, O. C., Lake, E. W., Gunaratne, G. S., Gallant, J. P., Fernie, M., Robertson, A. J., Marchant, J. S., Bold, T. D., Langlois, R. A., Matchett, W. E., Thiede, J. M., Shi, K., Yin, L., Moeller, N. H., Banerjee, S., Ferguson, L., Kovaleva, M., Porter, A. J., Aihara, H., LeBeau, A. M., and Barelle, C. J. (2021) Mechanisms of SARS-CoV-2 neutralization by shark variable new antigen receptors elucidated through X-ray crystallography. Nat Commun. 12, 7325

Ubah, O. C., Lake, E. W., Gunaratne, G. S., Gallant, J. P., Fernie, M., Robertson, A. J., Marchant, J. S., Bold, T. D., Langlois, R. A., Matchett, W. E., Thiede, J. M., Shi, K., Yin, L., Moeller, N. H., Banerjee, S., Ferguson, L., Kovaleva, M., Porter, A. J., Aihara, H., LeBeau, A. M., and Barelle, C. J. (2021) Mechanisms of SARS-CoV-2 neutralization by shark variable new antigen receptors elucidated through X-ray crystallography. Nat Commun. 12, 7325

Gu, W., Gao, S., Wang, H., Fleming, K. D., Hoffmann, R. M., Yang, J. Won, Patel, N. M., Choi, Y. Mi, Burke, J. E., Reue, K., and Airola, M. V. (2021) The middle lipin domain adopts a membrane-binding dimeric protein fold. Nat Commun. 12, 4718

Rapp, M., Guo, Y., Reddem, E. R., Yu, J., Liu, L., Wang, P., Cerutti, G., Katsamba, P., Bimela, J. S., Bahna, F. A., Mannepalli, S. M., Zhang, B., Kwong, P. D., Huang, Y., Ho, D. D., Shapiro, L., and Sheng, Z. (2021) Modular basis for potent SARS-CoV-2 neutralization by a prevalent VH1-2-derived antibody class. Cell Rep. 10.1016/j.celrep.2021.108950

Rapp, M., Guo, Y., Reddem, E. R., Yu, J., Liu, L., Wang, P., Cerutti, G., Katsamba, P., Bimela, J. S., Bahna, F. A., Mannepalli, S. M., Zhang, B., Kwong, P. D., Huang, Y., Ho, D. D., Shapiro, L., and Sheng, Z. (2021) Modular basis for potent SARS-CoV-2 neutralization by a prevalent VH1-2-derived antibody class. Cell Rep. 10.1016/j.celrep.2021.108950

Mulvaney, K. M., Blomquist, C., Acharya, N., Li, R., Ranaghan, M. J., O'Keefe, M., Rodriguez, D. J., Young, M. J., Kesar, D., Pal, D., Stokes, M., Nelson, A. J., Jain, S. S., Yang, A., Mullin-Bernstein, Z., Columbus, J., Bozal, F. K., Skepner, A., Raymond, D., LaRussa, S., McKinney, D. C., Freyzon, Y., Baidi, Y., Porter, D., Aguirre, A. J., Ianari, A., McMillan, B., and Sellers, W. R. (2021) Molecular basis for substrate recruitment to the PRMT5 methylosome. Mol Cell. 81, 3481-3495.e7

Mulvaney, K. M., Blomquist, C., Acharya, N., Li, R., Ranaghan, M. J., O'Keefe, M., Rodriguez, D. J., Young, M. J., Kesar, D., Pal, D., Stokes, M., Nelson, A. J., Jain, S. S., Yang, A., Mullin-Bernstein, Z., Columbus, J., Bozal, F. K., Skepner, A., Raymond, D., LaRussa, S., McKinney, D. C., Freyzon, Y., Baidi, Y., Porter, D., Aguirre, A. J., Ianari, A., McMillan, B., and Sellers, W. R. (2021) Molecular basis for substrate recruitment to the PRMT5 methylosome. Mol Cell. 81, 3481-3495.e7

Mulvaney, K. M., Blomquist, C., Acharya, N., Li, R., Ranaghan, M. J., O'Keefe, M., Rodriguez, D. J., Young, M. J., Kesar, D., Pal, D., Stokes, M., Nelson, A. J., Jain, S. S., Yang, A., Mullin-Bernstein, Z., Columbus, J., Bozal, F. K., Skepner, A., Raymond, D., LaRussa, S., McKinney, D. C., Freyzon, Y., Baidi, Y., Porter, D., Aguirre, A. J., Ianari, A., McMillan, B., and Sellers, W. R. (2021) Molecular basis for substrate recruitment to the PRMT5 methylosome. Mol Cell. 81, 3481-3495.e7

Silvaroli, J. A., Plau, J., Adams, C. H., Banerjee, S., Widjaja-Adhi, M. Airanthi K., Blaner, W. S., and Golczak, M. (2021) Molecular basis for the interaction of cellular retinol-binding protein 2 (CRBP2) with non-retinoid ligands. J Lipid Res. 10.1016/j.jlr.2021.100054

Silvaroli, J. A., Plau, J., Adams, C. H., Banerjee, S., Widjaja-Adhi, M. Airanthi K., Blaner, W. S., and Golczak, M. (2021) Molecular basis for the interaction of cellular retinol-binding protein 2 (CRBP2) with non-retinoid ligands. J Lipid Res. 10.1016/j.jlr.2021.100054

Dawson, C. D., Irwin, S. M., Backman, L. R. F., Le, C., Wang, J. X., Vennelakanti, V., Yang, Z., Kulik, H. J., Drennan, C. L., and Balskus, E. P. (2021) Molecular basis of C-S bond cleavage in the glycyl radical enzyme isethionate sulfite-lyase. Cell Chem Biol. 10.1016/j.chembiol.2021.03.001

Dawson, C. D., Irwin, S. M., Backman, L. R. F., Le, C., Wang, J. X., Vennelakanti, V., Yang, Z., Kulik, H. J., Drennan, C. L., and Balskus, E. P. (2021) Molecular basis of C-S bond cleavage in the glycyl radical enzyme isethionate sulfite-lyase. Cell Chem Biol. 10.1016/j.chembiol.2021.03.001

Borowska, M. T., Drees, C., Yarawsky, A. E., Viswanathan, M., Ryan, S. M., Bunker, J. J., Herr, A. B., Bendelac, A., and Adams, E. J. (2021) The molecular characterization of antibody binding to a superantigen-like protein from a commensal microbe. Proc Natl Acad Sci U S A. 10.1073/pnas.2023898118

Borowska, M. T., Drees, C., Yarawsky, A. E., Viswanathan, M., Ryan, S. M., Bunker, J. J., Herr, A. B., Bendelac, A., and Adams, E. J. (2021) The molecular characterization of antibody binding to a superantigen-like protein from a commensal microbe. Proc Natl Acad Sci U S A. 10.1073/pnas.2023898118

Borowska, M. T., Drees, C., Yarawsky, A. E., Viswanathan, M., Ryan, S. M., Bunker, J. J., Herr, A. B., Bendelac, A., and Adams, E. J. (2021) The molecular characterization of antibody binding to a superantigen-like protein from a commensal microbe. Proc Natl Acad Sci U S A. 10.1073/pnas.2023898118

Schnabl, J., Wang, J., Hohmann, U., Gehre, M., Batki, J., Andreev, V. I., Purkhauser, K., Fasching, N., Duchek, P., Novatchkova, M., Mechtler, K., Plaschka, C., Patel, D. J., and Brennecke, J. (2021) Molecular principles of Piwi-mediated cotranscriptional silencing through the dimeric SFiNX complex. Genes Dev. 35, 392-409

Schnabl, J., Wang, J., Hohmann, U., Gehre, M., Batki, J., Andreev, V. I., Purkhauser, K., Fasching, N., Duchek, P., Novatchkova, M., Mechtler, K., Plaschka, C., Patel, D. J., and Brennecke, J. (2021) Molecular principles of Piwi-mediated cotranscriptional silencing through the dimeric SFiNX complex. Genes Dev. 35, 392-409

Patchett, S., Lv, Z., Rut, W., Békés, M., Drag, M., Olsen, S. K., and Huang, T. T. (2021) A molecular sensor determines the ubiquitin substrate specificity of SARS-CoV-2 papain-like protease. Cell Rep. 36, 109754

Zahid, H., Buchholz, C. R., Singh, M., Ciccone, M. F., Chan, A., Nithianantham, S., Shi, K., Aihara, H., Fischer, M., Schönbrunn, E., Santos, C. O. Dos, Landry, J. W., and Pomerantz, W. C. K. (2021) New Design Rules for Developing Potent Cell-Active Inhibitors of the Nucleosome Remodeling Factor (NURF) via BPTF Bromodomain Inhibition. J Med Chem. 64, 13902-13917

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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
Massachusetts Institute of Technology
Memorial Sloan-Kettering Cancer Center
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.