https://nova.newcastle.edu.au/vital/access/ /manager/Index ${session.getAttribute("locale")} 5 Development of 1,8-naphthalimides as clathrin inhibitors https://nova.newcastle.edu.au/vital/access/ /manager/Repository/uon:21428 50 ≈ 18 μM). A second library targeting the 4-aminobenzyl moiety was developed, and four analogues displayed comparable activity (26, 27, 28, 34 with IC₅₀ values of 22, 16, 15, and 15 μM respectively) with a further four (24, 25, 32, 33) more active than 18 with IC₅₀ values of 10, 6.9, 12, and 10 μM, respectively. Docking studies rationalized the structure–activity relationship (SAR) with the biological data. 3-Sulfo-N-benzyl-1,8-naphthalimide, potassium salt (25) with an IC50 ≈ 6.9 μM, is the most potent clathrin terminal domain–amphiphysin inhibitor reported to date.]]> Sat 24 Mar 2018 08:05:47 AEDT ]]> Synthesis of the Pitstop family of clathrin inhibitors https://nova.newcastle.edu.au/vital/access/ /manager/Repository/uon:20625 Sat 24 Mar 2018 07:55:46 AEDT ]]> Clathrin terminal domain-ligand interactions regulate sorting of mannose 6-phosphate receptors mediated by AP-1 and GGA adaptors https://nova.newcastle.edu.au/vital/access/ /manager/Repository/uon:20674 Sat 24 Mar 2018 07:55:38 AEDT ]]> 5-Aryl-2-(naphtha-1-yl)sulfonamido-thiazol-4(5H)-ones as clathrin inhibitors https://nova.newcastle.edu.au/vital/access/ /manager/Repository/uon:28474 in silico docking studies. Docking studies predicted enhanced Pitstop® 2 family binding, not a loss of binding, within the Pistop® groove of the reported clathrin mutant invalidating recent assumptions of poor selectivity for this family of clathrin inhibitors.]]> Sat 24 Mar 2018 07:39:34 AEDT ]]>