22. Zhang, Q., Lindenberger, J., Parsons, R., Thakur, B., Parks, R., Park, C., Huang, X., Sammour, S., Janowska, K., Spence, T., Edwards, R., Martin, M., Williams, W., Gobeil, S., Montefiori, D., Korber, B., Saunders, K., Haynes, B., Henderson, R., Acharya, P. (2024) SARS-CoV-2 Omicron XBB Lineage Spike Structures, Conformations, Antigenicity, and Receptor Recognition. http://dx.doi.org/10.2139/ssrn.4761075
PDB IDs 8UKD,8UIR, 8UK1, 8UKF, 8V0L, 8V0M, 8V0N, 8V0O, 8V0P, 8V0Q, 8V0R, 8V0S, 8V0T, 8V0U, 8V0V, 8V0W, 8V0X, 9AYW, 9AYX, 9AYY
EMDB IDs 42302, 42342, 42352, 42353, 42860, 42861, 42862, 42863, 42864, 42866, 42867, 42868, 42869, 42870, 42871, 42872, 42873,
43422, 43423, 43451, 43452, 43453, 43460, 43461, 43462, 43463, 43464,44000, 44001, 44002, 44003, 44004, 44005, 44006,
44007.
21. Stalls, V., Lindenberger, J., Gobeil, S. M. C., Henderson, R., Parks, R., Barr, M., Deyton, M., Martin, M., Janowska, K., Huang, X., May, A., Speakman, M., Beaudoin, E., Edwards, R.J., Eaton, A., Montefiori, D.C., Williams, W., Saunders, K.O., Wiehe, K., Haynes, B.F., Acharya P. (2022) Cryo-EM structures of SARS-CoV-2 Omicron BA.2 Spike. Cell Reports. 39;13, 111009. https://doi.org/10.1016/j.celrep.2022.111009
PDB IDs 7UB0, 7UB5, 7UB6
EMDB IDs 26433, 26435, 26436, 26643 and 26647
20. *indicates co-first authorship: Gobeil, S.M.C.*, Henderson, R.*, Stalls, V.*, Janowska, K., Huang, X., May, A., Speakman, M., Beaudoin, E., Manne, K., Li, D., Parks, R., Barr, M., Deyton, M., Martin, M., Mansouri, K., Edwards, R.J., Sempowski, G.D., Saunders, K.O., Wiehe, K., Williams, W., Korber, B., Haynes, B.F., Acharya, P. (2022) Structural diversity of the SARS-CoV-2 Omicron spike, Mol. Cell. 82, 2050-2068.e6 https://doi.org/10.1016/j.molcel.2022.03.028
PDB IDs 7TF8, 7TL1, 7TEI, 7TL9, 7TGE, 7TOU, 7TOX, 7TOY, 7TOZ, 7TP0, 7TP1, 7TP2, 7TOV, 7TP7, 7TP8, 7TP9, 7TPA, 7TPC, 7TPE, 7TPF, 7TPH,
7TPL, 7TLA, 7TLB, 7TLC, 7TLD, 7THT and 7THE
EMDB IDs 25865, 25983, 25846, 25984, 25880, 26038, 26040, 26041, 26042, 26043, 26045, 26046, 26039, 26047, 26048, 26600, 26049,
26050, 26051, 26052, 26053, 26055, 26059, 25985, 25986, 25987, 25988, 25904 and 25893.
Crystal structure of DH1058 Fab bound to the SARS-CoV-2 fusion peptide PDB ID: 7TOW
19. Gobeil, S. M. C., Janowska, K., McDowell, S., Mansouri, K., Parks, R., Stalls, V., Kopp, M. F., Manne, K., Li, D., Wiehe, K., Saunders, K. O., Edwards, R. J., Korber, B., Haynes, B. F., Henderson, R. & Acharya, P. (2021) Effect of natural mutations of SARS-CoV-2 on spike structure, conformation, and antigenicity, Science. 373. https://doi.org/10.1126/science.abi6226
PDB IDs 7LWI, 7LWJ, 7LWK, 7LWL, 7LWM, 7LWN, 7LWO, 7LWP, 7LWQ, 7LWT, 7LWU, 7LWV, 7LWS, 7LWW, 7LYK, 7LYL, 7LYM, 7LYN, 7LYO, 7LYP, 7LYQ
EMDB IDs 23546, 23547, 23548, 23549, 23550, 23551, 23552, 23553, 23554, 23556, 23557, 23558, 23555, 23559, 23593, 23594, 23595,
23596, 23597, 23598, 23599
18. * indicates co-first authorship: Martinez, D. R.*, Schafer, A.*, Gobeil, S.M.C.*, Li, D.*, De la Cruz, G., Parks, R., Lu, X., Barr, M., Stalls, V., Janowska, K., Beaudoin, E., Manne, K., Mansouri, K., Edwards, R. J., Cronin, K., Yount, B., Anasti, K., Montgomery, S. A., Tang, J., Golding, H., Shen, S., Zhou, T., Kwong, P. D., Graham, B. S., Mascola, J. R., Montefiori, D. C., Alam, S. M., Sempowski, G. D., Khurana, S., Wiehe, K., Saunders, K. O., Acharya, P., Haynes, B. F. & Baric, R. S. (2021) A broadly cross-reactive antibody neutralizes and protects against sarbecovirus challenge in mice, Science Translational Medicine, eabj7125. https://doi.org/10.1126/scitranslmed.abj7125
PDB ID 7SG4
EMD ID 25105
17. Gobeil, S. M. C., Janowska, K., McDowell, S., Mansouri, K., Parks, R., Manne, K., Stalls, V., Kopp, M. F., Henderson, R., Edwards, R. J., Haynes, B. F. & Acharya, P. (2021) D614G Mutation Alters SARS-CoV-2 Spike Conformation and Enhances Protease Cleavage at the S1/S2 Junction, Cell Reports. 34. https://doi.org/10.1016/j.celrep.2020.108630
PDB IDs 7KDG, 7KDH, 7KDK, 7KDL, 7KDI, 7KDJ, 7KE4, 7KE6, 7KE7, 7KE8, 7KE9, 7KEA, 7KEB, 7KEC
EMDB IDs 22821, 22822, 22825, 22826, 22823, 22824, 22831, 22832, 22833, 22834, 22835, 22835, 22837, 22838
16. Gobeil, S. M. C., Bobay, B. G., Juvvadi, P. R., Cole, D. C., Heitman, J., Steinbach, W. J., Venters, R. A. & Spicer, L. D. (2021) Leveraging Fungal and Human Calcineurin-Inhibitor Structures, Biophysical Data, and Dynamics to Design Selective and Nonimmunosuppressive FK506 Analogs, mBio. 12, e03000-21. https://doi.org/10.1128/mBio.03000-21
PDB IDs 6VRX, 6VCU, 6VCV, 6VCT
15. Saunders, K. O., Lee, E., Parks, R., Martinez, D. R., Li, D., Chen, H., Edwards, R. J., Gobeil, S.M.C, Barr, M., Mansouri, K., Alam, S. M., Sutherland, L. L., Cai, F., Sanzone, A. M., Berry, M., Manne, K., Bock, K. W., Minai, M., Nagata, B. M., Kapingidza, A. B., Azoitei, M., Tse, L. V., Scobey, T. D., Spreng, R. L., Rountree, R. W., DeMarco, C. T., Denny, T. N., Woods, C. W., Petzold, E. W., Tang, J., Oguin, T. H., Sempowski, G. D., Gagne, M., Douek, D. C., Tomai, M. A., Fox, C. B., Seder, R., Wiehe, K., Weissman, D., Pardi, N., Golding, H., Khurana, S., Acharya, P., Andersen, H., Lewis, M. G., Moore, I. N., Montefiori, D. C., Baric, R. S. & Haynes, B. F. (2021) Neutralizing antibody vaccine for pandemic and pre-emergent coronaviruses, Nature. 594, 553- 559. https://doi.org/10.1038/s41586-021-03594-0
14. Williams, W. B., Meyerhoff, R. R., Edwards, R. J., Li, H., Manne, K., Nicely, N. I., Henderson, R., Zhou, Y., Janowska, K., Mansouri, K., Gobeil, S.M.C, Evangelous, T., Hora, B., Berry, M., Abuahmad, A. 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., Moody, M. A., Wiehe, K., Bradley, T., Alam, S. 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. & Haynes, B. F. (2021) Fab-dimerized glycan-reactive antibodies are a structural category of natural antibodies, Cell. 184, 2955-2972.e25. https://doi.org/10.1016/j.cell.2021.04.042
13. Li, D., Edwards, R. J., Manne, K., Martinez, D. R., Schäfer, A., Alam, S. M., Wiehe, K., Lu, X., Parks, R., Sutherland, L. L., Oguin, T. H., McDanal, C., Perez, L. G., Mansouri, K., Gobeil, S. M. C., Janowska, K., Stalls, V., Kopp, M., Cai, F., Lee, E., Foulger, A., Hernandez, G. E., Sanzone, A., Tilahun, K., Jiang, C., Tse, L. V., Bock, K. W., Minai, M., Nagata, B. M., Cronin, K., Gee-Lai, V., Deyton, M., Barr, M., Von Holle, T., Macintyre, A. N., Stover, E., Feldman, J., Hauser, B. M., Caradonna, T. M., Scobey, T. D., Rountree, W., Wang, Y., Moody, M. A., Cain, D. W., DeMarco, C. T., Denny, T. N., Woods, C. W., Petzold, E. W., Schmidt, A. G., Teng, I. T., Zhou, T., Kwong, P. D., Mascola, J. R., Graham, B. S., Moore, I. N., Seder, R., Andersen, H., Lewis, M. G., Montefiori, D. C., Sempowski, G. D., Baric, R. S., Acharya, P., Haynes, B. F. & Saunders, K. O. (2021) In vitro and in vivo functions of SARS-CoV-2 infection-enhancing and neutralizing antibodies, Cell. 184, 4203-4219.e32. https://doi.org/10.1016/j.cell.2021.06.021
12. *indicates co-first authorship: Edwards, R. J.*, Mansouri, K.*, Stalls, V.*, Manne, K.*, Watts, B., Parks, R., Janowska, K., Gobeil, S. M. C., Kopp, M., Li, D., Lu, X., Mu, Z., Deyton, M., Oguin, T. H., Sprenz, J., Williams, W., Saunders, K. O., Montefiori, D., Sempowski, G. D., Henderson, R., Munir Alam, S., Haynes, B. F. & Acharya, P. (2021) Cold sensitivity of the SARS-CoV-2 spike ectodomain, Nature Structural & Molecular Biology. 28, 128-131. https://doi.org/10.1038/s41594-020-00547-5.
11. Weissman, D., Alameh, M.-G., de Silva, T., Collini, P., Hornsby, H., Brown, R., LaBranche, C. C., Edwards, R. J., Sutherland, L., Santra, S., Mansouri, K., Gobeil, S.M.C, McDanal, C., Pardi, N., Hengartner, N., Lin, P. J. C., Tam, Y., Shaw, P. A., Lewis, M. G., Boesler, C., Şahin, U., Acharya, P., Haynes, B. F., Korber, B. & Montefiori, D. C. (2021) D614G Spike Mutation Increases SARS CoV-2 Susceptibility to Neutralization, Cell Host & Microbe. 29, 23-31.e4. https://doi.org/10.1016/j.chom.2020.11.012.
10. Paquet-Côté, P.-A., Alejaldre, L., Lapointe Verreault, C., Gobeil, S. M. C., Lamoureux, R., Bédard, L., Normandeau, C.-O., Lemay-St-Denis, C., Pelletier, J. N. & Voyer, N. (2021) Development of sulfahydantoin derivatives as β-lactamase inhibitors, Bioorganic & Medicinal Chemistry Letters. 35. https://doi.org/10.1016/j.bmcl.2021.127781
9. Henderson, R., Edwards, R. J., Mansouri, K., Janowska, K., Stalls, V., Gobeil, S. M. C., Kopp, M., Li, D., Parks, R., Hsu, A. L., Borgnia, M. J., Haynes, B. F. & Acharya, P. (2020) Controlling the SARS-CoV-2 spike glycoprotein conformation, Nature Structural & Molecular Biology. 27, 925- 933. https://doi.org/10.1038/s41594-020-0479-4
8. Juvvadi, P. R., Bobay, B. G., Gobeil, S. M. C., Cole, D. C., Venters, R. A., Heitman, J., Spicer, L. D. & Steinbach, W. J. (2020) FKBP12 dimerization mutations effect FK506 binding and differentially alter calcineurin inhibition in the human pathogen Aspergillus fumigatus, Biochemical and Biophysical Research Communications. 526, 48-54. https://doi.org/10.1016/j.bbrc.2020.03.062
7. Juvvadi, P.R., Fox, D., Bobay, B., Hoy, M., Gobeil, S., Venters, R., Chang, Z., Lin, J., Averette, A., Cole, C., Barrington, B., Wheaton, J., Ciofani, M., Trzoss, M., Li, X., Lee, S., Chen, Y., Mutz, M., Spicer, L., Schumacher, M., Heitman, J., Steinbach, W. Harnessing calcineurin-FK506-FKBP12 crystal structures from invasive fungal pathogens to develop antifungal agents. Nat Commun 10, 4275 (2019). https://doi.org/10.1038/s41467-019-12199-1
6. Gobeil, S. M. C., Bobay, B. G., Spicer, L. D. & Venters, R. A. (2019) 15N, 13C and 1H resonance assignments of FKBP12 proteins from the pathogenic fungi Mucor circinelloides and Aspergillusfumigatus, Biomolecular NMR Assignments. 13, 207-212. https://doi.org/10.1007/s12104-019-09878-x
BioMagResBank IDs 27732, 27733, 27734, 27737, 27738 and 27739
5. Gobeil, S. M. C., Ebert, M. C. C. J. C., Park, J., Gagné, D., Doucet, N., Berghuis, A. M., Pleiss, J. & Pelletier, J. N. (2019) The Structural Dynamics of Engineered β-Lactamases Vary Broadly on Three Timescales yet Sustain Native Function, Scientific Reports. 9. https://doi.org/10.1038/s41598-019-42866-8
4. Gobeil, S. M. C., Gagné, D., Doucet, N. & Pelletier, J. N. (2016) 15N, 13C and 1H backbone resonance assignments of an artificially engineered TEM-1/PSE-4 class A β-lactamase chimera and its deconvoluted mutant, Biomolecular NMR Assignments. 10, 93-99. https://doi.org/10.1007/s12104-015-9645-8
BioMagResBank IDs 26590, 26586
3. Gobeil SMC, Clouthier CM, Park J, Gagne D, Berghuis AM, Doucet N and Pelletier JN. Maintenance of Native- like Protein Dynamics Many Not Be Required for Engineering Functional Proteins. Chemistry and Biology. 2014; 21(10): 1330-40. https://doi.org/10.1016/j.chembiol.2014.07.016
2. Clouthier CM, Morin S, Gobeil SMC, Doucet N, Blanchet J, Nguyen E, Gagne SM and Pelletier JN. Chimeric β- Lactamases: Global Conservation of Parental Function and Fast Time-scale Dynamics with Increased Slow Motions. PLoS One. 2012; 7(12): e52283. https://doi.org/10.1371/journal.pone.0052283
1. Morin S, Clouthier C, Gobeil SMC, Pelletier JN and Gagne SM. Backbone Resonance Assignments of an Artificially Engineered TEM1/PSE4 Class A β-Lactamase Chimera, Biomolecular NMR Assignments. 2010; 4(2): 127-30. https://doi.org/10.1007/s12104-010-9227-8
BioMagResBank ID 16598
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