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2021

Landor, S. K. J., Santio, N. M., Eccleshall, W. B., Paramonov, V. M., Gagliani, E. K., Hall, D., Jin, S. - B., Dahlström, K. M., Salminen, T. A., Rivero-Müller, A., Lendahl, U., Kovall, R. A., Koskinen, P. J., and Sahlgren, C. (2021) PIM-induced phosphorylation of Notch3 promotes breast cancer tumorigenicity in a CSL-independent fashion. J Biol Chem. 10.1016/j.jbc.2021.100593

Landor, S. K. J., Santio, N. M., Eccleshall, W. B., Paramonov, V. M., Gagliani, E. K., Hall, D., Jin, S. - B., Dahlström, K. M., Salminen, T. A., Rivero-Müller, A., Lendahl, U., Kovall, R. A., Koskinen, P. J., and Sahlgren, C. (2021) PIM-induced phosphorylation of Notch3 promotes breast cancer tumorigenicity in a CSL-independent fashion. J Biol Chem. 10.1016/j.jbc.2021.100593

Landor, S. K. J., Santio, N. M., Eccleshall, W. B., Paramonov, V. M., Gagliani, E. K., Hall, D., Jin, S. - B., Dahlström, K. M., Salminen, T. A., Rivero-Müller, A., Lendahl, U., Kovall, R. A., Koskinen, P. J., and Sahlgren, C. (2021) PIM-induced phosphorylation of Notch3 promotes breast cancer tumorigenicity in a CSL-independent fashion. J Biol Chem. 10.1016/j.jbc.2021.100593

Zhang, C. - H., Stone, E. A., Deshmukh, M., Ippolito, J. A., Ghahremanpour, M. M., Tirado-Rives, J., Spasov, K. A., Zhang, S., Takeo, Y., Kudalkar, S. N., Liang, Z., Isaacs, F., Lindenbach, B., Miller, S. J., Anderson, K. S., and Jorgensen, W. L. (2021) Potent Noncovalent Inhibitors of the Main Protease of SARS-CoV-2 from Molecular Sculpting of the Drug Perampanel Guided by Free Energy Perturbation Calculations. ACS Cent Sci. 7, 467-475

Zhang, C. - H., Stone, E. A., Deshmukh, M., Ippolito, J. A., Ghahremanpour, M. M., Tirado-Rives, J., Spasov, K. A., Zhang, S., Takeo, Y., Kudalkar, S. N., Liang, Z., Isaacs, F., Lindenbach, B., Miller, S. J., Anderson, K. S., and Jorgensen, W. L. (2021) Potent Noncovalent Inhibitors of the Main Protease of SARS-CoV-2 from Molecular Sculpting of the Drug Perampanel Guided by Free Energy Perturbation Calculations. ACS Cent Sci. 7, 467-475

Cerutti, G., Guo, Y., Zhou, T., Gorman, J., Lee, M., Rapp, M., Reddem, E. R., Yu, J., Bahna, F., Bimela, J., Huang, Y., Katsamba, P. S., Liu, L., Nair, M. S., Rawi, R., Olia, A. S., Wang, P., Zhang, B., Chuang, G. - Y., Ho, D. D., Sheng, Z., Kwong, P. D., and Shapiro, L. (2021) Potent SARS-CoV-2 neutralizing antibodies directed against spike N-terminal domain target a single supersite. Cell Host Microbe. 10.1016/j.chom.2021.03.005

Cerutti, G., Guo, Y., Zhou, T., Gorman, J., Lee, M., Rapp, M., Reddem, E. R., Yu, J., Bahna, F., Bimela, J., Huang, Y., Katsamba, P. S., Liu, L., Nair, M. S., Rawi, R., Olia, A. S., Wang, P., Zhang, B., Chuang, G. - Y., Ho, D. D., Sheng, Z., Kwong, P. D., and Shapiro, L. (2021) Potent SARS-CoV-2 neutralizing antibodies directed against spike N-terminal domain target a single supersite. Cell Host Microbe. 10.1016/j.chom.2021.03.005

Castel, P., Dharmaiah, S., Sale, M. J., Messing, S., Rizzuto, G., Cuevas-Navarro, A., Cheng, A., Trnka, M. J., Urisman, A., Esposito, D., Simanshu, D. K., and McCormick, F. (2021) RAS interaction with Sin1 is dispensable for mTORC2 assembly and activity. Proc Natl Acad Sci U S A. 10.1073/pnas.2103261118

Castel, P., Dharmaiah, S., Sale, M. J., Messing, S., Rizzuto, G., Cuevas-Navarro, A., Cheng, A., Trnka, M. J., Urisman, A., Esposito, D., Simanshu, D. K., and McCormick, F. (2021) RAS interaction with Sin1 is dispensable for mTORC2 assembly and activity. Proc Natl Acad Sci U S A. 10.1073/pnas.2103261118

Torabi, S. - F., Vaidya, A. T., Tycowski, K. T., DeGregorio, S. J., Wang, J., Di Shu, M. -, Steitz, T. A., and Steitz, J. A. (2021) RNA stabilization by a poly(A) tail 3'-end binding pocket and other modes of poly(A)-RNA interaction. Science. 10.1126/science.abe6523

Torabi, S. - F., Vaidya, A. T., Tycowski, K. T., DeGregorio, S. J., Wang, J., Di Shu, M. -, Steitz, T. A., and Steitz, J. A. (2021) RNA stabilization by a poly(A) tail 3'-end binding pocket and other modes of poly(A)-RNA interaction. Science. 10.1126/science.abe6523

Shi, F., Mendrola, J. M., Sheetz, J. B., Wu, N., Sommer, A., Speer, K. F., Noordermeer, J. N., Kan, Z. - Y., Perry, K., S Englander, W., Stayrook, S. E., Fradkin, L. G., and Lemmon, M. A. (2021) ROR and RYK extracellular region structures suggest that receptor tyrosine kinases have distinct WNT-recognition modes. Cell Rep. 37, 109834

Shi, F., Mendrola, J. M., Sheetz, J. B., Wu, N., Sommer, A., Speer, K. F., Noordermeer, J. N., Kan, Z. - Y., Perry, K., S Englander, W., Stayrook, S. E., Fradkin, L. G., and Lemmon, M. A. (2021) ROR and RYK extracellular region structures suggest that receptor tyrosine kinases have distinct WNT-recognition modes. Cell Rep. 37, 109834

Shi, F., Mendrola, J. M., Sheetz, J. B., Wu, N., Sommer, A., Speer, K. F., Noordermeer, J. N., Kan, Z. - Y., Perry, K., S Englander, W., Stayrook, S. E., Fradkin, L. G., and Lemmon, M. A. (2021) ROR and RYK extracellular region structures suggest that receptor tyrosine kinases have distinct WNT-recognition modes. Cell Rep. 37, 109834

Shi, F., Mendrola, J. M., Sheetz, J. B., Wu, N., Sommer, A., Speer, K. F., Noordermeer, J. N., Kan, Z. - Y., Perry, K., S Englander, W., Stayrook, S. E., Fradkin, L. G., and Lemmon, M. A. (2021) ROR and RYK extracellular region structures suggest that receptor tyrosine kinases have distinct WNT-recognition modes. Cell Rep. 37, 109834

Shi, F., Mendrola, J. M., Sheetz, J. B., Wu, N., Sommer, A., Speer, K. F., Noordermeer, J. N., Kan, Z. - Y., Perry, K., S Englander, W., Stayrook, S. E., Fradkin, L. G., and Lemmon, M. A. (2021) ROR and RYK extracellular region structures suggest that receptor tyrosine kinases have distinct WNT-recognition modes. Cell Rep. 37, 109834

Clark, S. A., Clark, L. E., Pan, J., Coscia, A., McKay, L. G. A., Shankar, S., Johnson, R. I., Griffiths, A., and Abraham, J. (2021) SARS-CoV-2 evolution in an immunocompromised host reveals shared neutralization escape mechanisms. Cell. 10.1101/2020.11.13.381533

Wybenga-Groot, L. E., Tench, A. J., Simpson, C. D., St Germain, J., Raught, B., Moran, M. F., and C McGlade, J. (2021) SLAP2 Adaptor Binding Disrupts c-CBL Autoinhibition to Activate Ubiquitin Ligase Function. J Mol Biol. 433, 166880

Wybenga-Groot, L. E., Tench, A. J., Simpson, C. D., St Germain, J., Raught, B., Moran, M. F., and C McGlade, J. (2021) SLAP2 Adaptor Binding Disrupts c-CBL Autoinhibition to Activate Ubiquitin Ligase Function. J Mol Biol. 433, 166880

Jones, J. C., Banerjee, R., Shi, K., Semonis, M. M., Aihara, H., Pomerantz, W. C. K., and Lipscomb, J. D. (2021) Soluble Methane Monooxygenase Component Interactions Monitored by F NMR. Biochemistry. 60, 1995-2010

Jones, J. C., Banerjee, R., Shi, K., Semonis, M. M., Aihara, H., Pomerantz, W. C. K., and Lipscomb, J. D. (2021) Soluble Methane Monooxygenase Component Interactions Monitored by F NMR. Biochemistry. 60, 1995-2010

Valentino, H., Korasick, D. A., Bohac, T. J., Shapiro, J. A., Wencewicz, T. A., Tanner, J. J., and Sobrado, P. (2021) Structural and Biochemical Characterization of the Flavin-Dependent Siderophore-Interacting Protein from . ACS Omega. 6, 18537-18547

Valentino, H., Korasick, D. A., Bohac, T. J., Shapiro, J. A., Wencewicz, T. A., Tanner, J. J., and Sobrado, P. (2021) Structural and Biochemical Characterization of the Flavin-Dependent Siderophore-Interacting Protein from . ACS Omega. 6, 18537-18547

Bowen, N. E., Temple, J., Shepard, C., Oo, A., Arizaga, F., Kapoor-Vazirani, P., Persaud, M., Yu, C. H., Kim, D. - H., Schinazi, R. F., Ivanov, D. N., Diaz-Griffero, F., Yu, D. S., Xiong, Y., and Kim, B. (2021) Structural and functional characterization explains loss of dNTPase activity of the cancer-specific R366C/H mutant SAMHD1 proteins. J Biol Chem. 10.1016/j.jbc.2021.101170

Bowen, N. E., Temple, J., Shepard, C., Oo, A., Arizaga, F., Kapoor-Vazirani, P., Persaud, M., Yu, C. H., Kim, D. - H., Schinazi, R. F., Ivanov, D. N., Diaz-Griffero, F., Yu, D. S., Xiong, Y., and Kim, B. (2021) Structural and functional characterization explains loss of dNTPase activity of the cancer-specific R366C/H mutant SAMHD1 proteins. J Biol Chem. 10.1016/j.jbc.2021.101170

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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.