Snapshots of ligand entry, malleable binding and induced helical movement in P-glycoprotein

по Szewczyk, Paul, Tao, Houchao, McGrath, Aaron P., Villaluz, Mark, Rees, Steven D., Lee, Sung Chang, Doshi, Rupak, Urbatsch, Ina L., Zhang, Qinghai, Chang, Geoffrey
Опубликовано в: Acta Crystallogr D Biol Crystallogr (2015)

Structural basis for GPCR-independent activation of heterotrimeric Gi proteins

по Kalogriopoulos, Nicholas A., Rees, Steven D., Ngo, Tony, Kopcho, Noah J., Ilatovskiy, Andrey V., Sun, Nina, Komives, Elizabeth A., Chang, Geoffrey, Ghosh, Pradipta, Kufareva, Irina
Опубликовано в: Proc Natl Acad Sci U S A (2019)

Global marine pollutants inhibit P-glycoprotein: Environmental levels, inhibitory effects, and cocrystal structure

по Nicklisch, Sascha C. T., Rees, Steven D., McGrath, Aaron P., Gökirmak, Tufan, Bonito, Lindsay T., Vermeer, Lydia M., Cregger, Cristina, Loewen, Greg, Sandin, Stuart, Chang, Geoffrey, Hamdoun, Amro
Опубликовано в: Sci Adv (2016)

Gut bacteria responding to dietary change encode sialidases that exhibit preference for red meat-associated carbohydrates

по Zaramela, Livia S., Martino, Cameron, Alisson-Silva, Frederico, Rees, Steven D., Diaz, Sandra L., Chuzel, Léa, Ganatra, Mehul B., Taron, Christopher H., Secrest, Patrick, Zuñiga, Cristal, Huang, Jianbo, Siegel, Dionicio, Chang, Geoffrey, Varki, Ajit, Zengler, Karsten
Опубликовано в: Nat Microbiol (2019)

Cryo-EM structure of OSCA1.2 from Oryza sativa elucidates the mechanical basis of potential membrane hyperosmolality gating

по Maity, Koustav, Heumann, John M., McGrath, Aaron P., Kopcho, Noah J., Hsu, Po-Kai, Lee, Chang-Wook, Mapes, James H., Garza, Denisse, Krishnan, Srinivasan, Morgan, Garry P., Hendargo, Kevin J., Klose, Thomas, Rees, Steven D., Medrano-Soto, Arturo, Saier, Milton H., Piñeros, Miguel, Komives, Elizabeth A., Schroeder, Julian I., Chang, Geoffrey, Stowell, Michael H. B.
Опубликовано в: Proc Natl Acad Sci U S A (2019)