https://ogma.newcastle.edu.au/vital/access/ /manager/Index ${session.getAttribute("locale")} 5 https://ogma.newcastle.edu.au/vital/access/ /manager/Repository/uon:13742 Wed 11 Apr 2018 16:49:24 AEST ]]> https://ogma.newcastle.edu.au/vital/access/ /manager/Repository/uon:37457 Wed 02 Mar 2022 14:26:12 AEDT ]]> https://ogma.newcastle.edu.au/vital/access/ /manager/Repository/uon:19083 Sat 24 Mar 2018 08:05:24 AEDT ]]> https://ogma.newcastle.edu.au/vital/access/ /manager/Repository/uon:20774 6 by cNLS Mapper), while 8 nuclear proteins lacked any cNLS. In addition, we developed a new strategy to predict which cargoes bind to importin a through the conserved C-terminal acidic domain (ARM repeats 9-10), and provided functional validation of a predicted importin α C-terminal binding segment in Senataxin and Smarca4. Evaluation of this set of candidate binding partners from spermatogenic cells using several bioinformatics approaches provides new evidence that individual importin αs may serve unique and nonredundant roles in mediating cellular differentiation.]]> Sat 24 Mar 2018 08:00:22 AEDT ]]> https://ogma.newcastle.edu.au/vital/access/ /manager/Repository/uon:19602 Sat 24 Mar 2018 07:58:23 AEDT ]]>