https://nova.newcastle.edu.au/vital/access/ /manager/Index ${session.getAttribute("locale")} 5 https://nova.newcastle.edu.au/vital/access/ /manager/Repository/uon:20160 36-fold reduced activity against rings, suggesting that they can discriminate between helical or ring oligomerization states. 4a and 6a inhibited dynamin-dependent endocytosis of transferrin in multiple cell types (IC50 of 5.7 and 5.8 μM, respectively), at least sixfold more potently than dynasore, but had no effect on dynamin-independent endocytosis of cholera toxin. 4a also reduced synaptic vesicle endocytosis and activity-dependent bulk endocytosis in cultured neurons and synaptosomes. Overall, 4a and 6a are improved and versatile helical dynamin and endocytosis inhibitors in terms of potency, non-specific binding and cytotoxicity. The data further suggest that the ring oligomerization state of dynamin is not required for clathrin-mediated endocytosis.]]> Tue 24 Aug 2021 14:23:34 AEST ]]> https://nova.newcastle.edu.au/vital/access/ /manager/Repository/uon:11336 Sat 24 Mar 2018 08:13:29 AEDT ]]> https://nova.newcastle.edu.au/vital/access/ /manager/Repository/uon:17425 Sat 24 Mar 2018 08:01:39 AEDT ]]> https://nova.newcastle.edu.au/vital/access/ /manager/Repository/uon:19893 Sat 24 Mar 2018 07:57:02 AEDT ]]>