Stewart, Cameron

Structural basis of SARS-CoV-2 Omicron immune evasion and receptor engagement

McCallum, M., Czudnochowski, N., Rosen, L. E., Zepeda, S. K., Bowen, J. E., Walls, A. C., Hauser, K., Joshi, A., Stewart, C., Dillen, J. R., et al. (2022) · Science

SARS-CoV-2 and COVID-19 Researchvaccines and immunoinformatics approaches

Cited by 535

Imprinted antibody responses against SARS-CoV-2 Omicron sublineages

Park, Y.-J., Pinto, D., Walls, A. C., Liu, Z., De Marco, A., Benigni, F., Zatta, F., Silacci-Fregni, C., Bassi, J., Sprouse, K. R., et al. (2022) · Science

SARS-CoV-2 and COVID-19 Researchvaccines and immunoinformatics approaches

Cited by 251

A broadly generalizable stabilization strategy for sarbecovirus fusion machinery vaccines

Lee, J., Stewart, C., Schäfer, A., Leaf, E. M., Park, Y.-J., Asarnow, D., Powers, J. M., Treichel, C., Sprouse, K. R., Corti, D., et al. (2024) · Nature Communications

SARS-CoV-2 and COVID-19 Researchvaccines and immunoinformatics approaches

Cited by 23

Fusion crystallization reveals the behavior of both the 1TEL crystallization chaperone and the TNK1 UBA domain

Nawarathnage, S., Tseng, Y. J., Soleimani, S., Smith, T., Pedroza Romo, M. J., Abiodun, W. O., Egbert, C. M., Madhusanka, D., Bunn, D., Woods, B., et al. (2023) · Structure

Enzyme Structure and FunctionUbiquitin and proteasome pathways

Cited by 6

Fusion crystallization reveals the behavior of both the 1TEL crystallization chaperone and the TNK1 UBA domain

Nawarathnage, S., Tseng, Y. J., Soleimani, S., Smith, T., Pedroza Romo, M. J., Abiodun, W. O., Egbert, C. M., Madhusanka, D., Bunn, D., Woods, B., et al. (2023) · Structure

Enzyme Structure and FunctionUbiquitin and proteasome pathways

Cited by 6

Functional and antigenic constraints on the Nipah virus fusion protein

Larsen, B. B., Harari, S., Gen, R., Stewart, C., Veesler, D., & Bloom, J. D. (2025) · Proceedings of the National Academy of Sciences

Virology and Viral DiseasesSARS-CoV-2 and COVID-19 Research

Cited by 3