The prolyl isomerase, FKBP25, interacts with RNA-engaged nucleolin and the pre-60S ribosomal subunit

Por Gudavicius, Geoff, Dilworth, David, Serpa, Jason J., Sessler, Nicole, Petrotchenko, Evgeniy V., Borchers, Christoph H., Nelson, Christopher J.
Publicado em 2014

Basic surface features of nuclear FKBPs facilitate chromatin binding

Por Leung, Andrew, Jardim, Francy-Pesek, Savic, Neda, Monneau, Yoan R., González-Romero, Rodrigo, Gudavicius, Geoff, Eirin-Lopez, Jose M., Bartke, Till, Mackereth, Cameron D., Ausió, Juan, Nelson, Christopher J.
Publicado no Sci Rep (2017)

The basic tilted helix bundle domain of the prolyl isomerase FKBP25 is a novel double-stranded RNA binding module

Por Dilworth, David, Upadhyay, Santosh K., Bonnafous, Pierre, Edoo, Amiirah Bibi, Bourbigot, Sarah, Pesek-Jardim, Francy, Gudavicius, Geoff, Serpa, Jason J., Petrotchenko, Evgeniy V., Borchers, Christoph H., Nelson, Christopher J., Mackereth, Cameron D.
Publicado no Nucleic Acids Res (2017)