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F
Williams, W. B., R Meyerhoff, R., Edwards, R. J., Li, H., Manne, K., Nicely, N. I., Henderson, R., Zhou, Y., Janowska, K., Mansouri, K., Gobeil, S., Evangelous, T., Hora, B., Berry, M., A Abuahmad, Y., Sprenz, J., Deyton, M., Stalls, V., Kopp, M., Hsu, A. L., Borgnia, M. J., Stewart-Jones, G. B. E., Lee, M. S., Bronkema, N., M Moody, A., Wiehe, K., Bradley, T., S Alam, M., Parks, R. J., Foulger, A., Oguin, T., Sempowski, G. D., Bonsignori, M., LaBranche, C. C., Montefiori, D. C., Seaman, M., Santra, S., Perfect, J., Francica, J. R., Lynn, G. M., Aussedat, B., Walkowicz, W. E., Laga, R., Kelsoe, G., Saunders, K. O., Fera, D., Kwong, P. D., Seder, R. A., Bartesaghi, A., Shaw, G. M., Acharya, P., and Haynes, B. F. (2021) Fab-dimerized glycan-reactive antibodies are a structural category of natural antibodies. Cell. 184, 2955-2972.e25
Williams, W. B., R Meyerhoff, R., Edwards, R. J., Li, H., Manne, K., Nicely, N. I., Henderson, R., Zhou, Y., Janowska, K., Mansouri, K., Gobeil, S., Evangelous, T., Hora, B., Berry, M., A Abuahmad, Y., Sprenz, J., Deyton, M., Stalls, V., Kopp, M., Hsu, A. L., Borgnia, M. J., Stewart-Jones, G. B. E., Lee, M. S., Bronkema, N., M Moody, A., Wiehe, K., Bradley, T., S Alam, M., Parks, R. J., Foulger, A., Oguin, T., Sempowski, G. D., Bonsignori, M., LaBranche, C. C., Montefiori, D. C., Seaman, M., Santra, S., Perfect, J., Francica, J. R., Lynn, G. M., Aussedat, B., Walkowicz, W. E., Laga, R., Kelsoe, G., Saunders, K. O., Fera, D., Kwong, P. D., Seder, R. A., Bartesaghi, A., Shaw, G. M., Acharya, P., and Haynes, B. F. (2021) Fab-dimerized glycan-reactive antibodies are a structural category of natural antibodies. Cell. 184, 2955-2972.e25
Williams, W. B., R Meyerhoff, R., Edwards, R. J., Li, H., Manne, K., Nicely, N. I., Henderson, R., Zhou, Y., Janowska, K., Mansouri, K., Gobeil, S., Evangelous, T., Hora, B., Berry, M., A Abuahmad, Y., Sprenz, J., Deyton, M., Stalls, V., Kopp, M., Hsu, A. L., Borgnia, M. J., Stewart-Jones, G. B. E., Lee, M. S., Bronkema, N., M Moody, A., Wiehe, K., Bradley, T., S Alam, M., Parks, R. J., Foulger, A., Oguin, T., Sempowski, G. D., Bonsignori, M., LaBranche, C. C., Montefiori, D. C., Seaman, M., Santra, S., Perfect, J., Francica, J. R., Lynn, G. M., Aussedat, B., Walkowicz, W. E., Laga, R., Kelsoe, G., Saunders, K. O., Fera, D., Kwong, P. D., Seder, R. A., Bartesaghi, A., Shaw, G. M., Acharya, P., and Haynes, B. F. (2021) Fab-dimerized glycan-reactive antibodies are a structural category of natural antibodies. Cell. 184, 2955-2972.e25
E
Moremen, K. W., Ramiah, A., Stuart, M., Steel, J., Meng, L., Forouhar, F., Moniz, H. A., Gahlay, G., Gao, Z., Chapla, D., Wang, S., Yang, J. - Y., Prabhakar, P. Kumar, Johnson, R., Rosa, M. Dela, Geisler, C., Nairn, A. V., Seetharaman, J., Wu, S. - C., Tong, L., Gilbert, H. J., LaBaer, J., and Jarvis, D. L. (2017) Expression system for structural and functional studies of human glycosylation enzymes. Nat Chem Biol. 10.1038/nchembio.2539
Said, M. Y., Kang, C. S., Wang, S., Sheffler, W., Salveson, P. J., Bera, A. K., Kang, A., Nguyen, H., Ballard, R., Li, X., Bai, H., Stewart, L., Levine, P., and Baker, D. (2022) Exploration of Structured Symmetric Cyclic Peptides as Ligands for Metal-Organic Frameworks. Chem Mater. 34, 9736-9744
Said, M. Y., Kang, C. S., Wang, S., Sheffler, W., Salveson, P. J., Bera, A. K., Kang, A., Nguyen, H., Ballard, R., Li, X., Bai, H., Stewart, L., Levine, P., and Baker, D. (2022) Exploration of Structured Symmetric Cyclic Peptides as Ligands for Metal-Organic Frameworks. Chem Mater. 34, 9736-9744
Krauthammer, M., Kong, Y., Ha, B. Hak, Evans, P., Bacchiocchi, A., McCusker, J. P., Cheng, E., Davis, M. J., Goh, G., Choi, M., Ariyan, S., Narayan, D., Dutton-Regester, K., Capatana, A., Holman, E. C., Bosenberg, M., Sznol, M., Kluger, H. M., Brash, D. E., Stern, D. F., Materin, M. A., Lo, R. S., Mane, S., Ma, S., Kidd, K. K., Hayward, N. K., Lifton, R. P., Schlessinger, J., Boggon, T. J., and Halaban, R. (2012) Exome sequencing identifies recurrent somatic RAC1 mutations in melanoma. Nat Genet. 44, 1006-14
Krauthammer, M., Kong, Y., Ha, B. Hak, Evans, P., Bacchiocchi, A., McCusker, J. P., Cheng, E., Davis, M. J., Goh, G., Choi, M., Ariyan, S., Narayan, D., Dutton-Regester, K., Capatana, A., Holman, E. C., Bosenberg, M., Sznol, M., Kluger, H. M., Brash, D. E., Stern, D. F., Materin, M. A., Lo, R. S., Mane, S., Ma, S., Kidd, K. K., Hayward, N. K., Lifton, R. P., Schlessinger, J., Boggon, T. J., and Halaban, R. (2012) Exome sequencing identifies recurrent somatic RAC1 mutations in melanoma. Nat Genet. 44, 1006-14
McGee, J. H., Shim, S. Youn, Lee, S. - J., Swanson, P. K., Jiang, Y., Durney, M. A., and Verdine, G. L. (2017) Exceptionally high-affinity Ras binders that remodel its effector domain. J Biol Chem. 10.1074/jbc.M117.816348
Huang, J., Liu, X., Sun, Y., Li, Z., Lin, M. - H., Hamilton, K., Mandel, C. R., Sandmeir, F., Conti, E., Oyala, P. H., and Tong, L. (2023) An examination of the metal ion content in the active sites of human endonucleases CPSF73 and INTS11. J Biol Chem. 299, 103047
Huang, J., Liu, X., Sun, Y., Li, Z., Lin, M. - H., Hamilton, K., Mandel, C. R., Sandmeir, F., Conti, E., Oyala, P. H., and Tong, L. (2023) An examination of the metal ion content in the active sites of human endonucleases CPSF73 and INTS11. J Biol Chem. 299, 103047
Huang, J., Liu, X., Sun, Y., Li, Z., Lin, M. - H., Hamilton, K., Mandel, C. R., Sandmeir, F., Conti, E., Oyala, P. H., and Tong, L. (2023) An examination of the metal ion content in the active sites of human endonucleases CPSF73 and INTS11. J Biol Chem. 299, 103047
Ren, X., Gelinas, A. D., Linehan, M., Iwasaki, A., Wang, W., Janjic, N., and Pyle, A. Marie (2021) Evolving A RIG-I Antagonist: A Modified DNA Aptamer Mimics Viral RNA. J Mol Biol. 433, 167227
Wang, F., Li, L., Dou, Y., Shi, R., Duan, X., Liu, H., Zhang, J., Liu, D. D., Wu, J., He, Y., Lan, J., Lu, B., Feng, H., and Yan, J. (2022) Etesevimab in combination with JS026 neutralizing SARS-CoV-2 and its variants. Emerg Microbes Infect. 11, 548-551
Wang, F., Li, L., Dou, Y., Shi, R., Duan, X., Liu, H., Zhang, J., Liu, D. D., Wu, J., He, Y., Lan, J., Lu, B., Feng, H., and Yan, J. (2022) Etesevimab in combination with JS026 neutralizing SARS-CoV-2 and its variants. Emerg Microbes Infect. 11, 548-551
Wang, F., Li, L., Dou, Y., Shi, R., Duan, X., Liu, H., Zhang, J., Liu, D. D., Wu, J., He, Y., Lan, J., Lu, B., Feng, H., and Yan, J. (2022) Etesevimab in combination with JS026 neutralizing SARS-CoV-2 and its variants. Emerg Microbes Infect. 11, 548-551
Wang, F., Li, L., Dou, Y., Shi, R., Duan, X., Liu, H., Zhang, J., Liu, D. D., Wu, J., He, Y., Lan, J., Lu, B., Feng, H., and Yan, J. (2022) Etesevimab in combination with JS026 neutralizing SARS-CoV-2 and its variants. Emerg Microbes Infect. 11, 548-551
Wang, F., Li, L., Dou, Y., Shi, R., Duan, X., Liu, H., Zhang, J., Liu, D. D., Wu, J., He, Y., Lan, J., Lu, B., Feng, H., and Yan, J. (2022) Etesevimab in combination with JS026 neutralizing SARS-CoV-2 and its variants. Emerg Microbes Infect. 11, 548-551
Wyatt, S., Glover, K., Dasanna, S., Lewison, M., González-García, M., Colbert, C. L., and Sinha, S. C. (2023) Epstein-Barr Virus Encoded BCL2, BHRF1, Downregulates Autophagy by Noncanonical Binding of BECN1. Biochemistry. 62, 2934-2951
Smith, M. A., and Lancaster, K. M. (2018) The Eponymous Cofactors in Cytochrome P460s from Ammonia-Oxidizing Bacteria Are Iron Porphyrinoids Whose Macrocycles Are Dibasic. Biochemistry. 57, 334-343
Jenson, J. M., Ryan, J. A., Grant, R. A., Letai, A., and Keating, A. E. (2017) Epistatic mutations in PUMA BH3 drive an alternate binding mode to potently and selectively inhibit anti-apoptotic Bfl-1. Elife. 10.7554/eLife.25541
Levin, E. J., Kondrashov, D. A., Wesenberg, G. E., and Phillips, G. N. (2007) Ensemble refinement of protein crystal structures: validation and application. Structure. 15, 1040-52
Nocula-Lugowska, M., Lugowski, M., Salgia, R., and Kossiakoff, A. A. (2015) Engineering Synthetic Antibody Inhibitors Specific for LD2 or LD4 Motifs of Paxillin. J Mol Biol. 427, 2532-2547
Ruan, B., London, V., Fisher, K. E., D Gallagher, T., and Bryan, P. N. (2008) Engineering substrate preference in subtilisin: structural and kinetic analysis of a specificity mutant. Biochemistry. 47, 6628-36
Noh, K. - M., Wang, H., Kim, H. R., Wenderski, W., Fang, F., Li, C. H., Dewell, S., Hughes, S. H., Melnick, A. M., Patel, D. J., Li, H., and C Allis, D. (2015) Engineering of a Histone-Recognition Domain in Dnmt3a Alters the Epigenetic Landscape and Phenotypic Features of Mouse ESCs. Mol Cell. 59, 89-103

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