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Adam McCluskey, James A. Daniel, Gordana Hadzic, Ngoc Chau, Emma L. Clayton, Anna Mariana, Ainslie Whiting, Nick N. Gorgani, Jonathan Lloyd, Annie Quan, Lia Moshkanbaryans, Sai Krishnan, Swetha Perera, Megan Chircop, Lisa von Kleist, Andrew B. McGeachie, Mark T. Howes, Robert G. Parton, Michael Campbell, Jennette A. Sakoff, Xuefeng Wang, Jian-Yuan Sun, Mark J. Robertson, Fiona M. Deane, Tam H. Nguyen, Frederic A. Meunier, Michael A. Cousin and Phillip J. Robinson Building a Better Dynasore: The Dyngo Compounds Potently Inhibit Dynamin and Endocytosis Traffic 14

Article first published online: 9 OCT 2013 | DOI: 10.1111/tra.12119

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Dynamin is essential for clathrin-mediated endocytosis (CME). We describe the Dyngo™ series of dynamin inhibitors with greatly improved potency, reduced cytotoxicity and reduced detergent binding compared to their parent, dynasore. Dyngo compound 4a is 37-fold more potent for dynamin inhibition and at least sixfold more potent for CME inhibition in cells and nerve terminals. This series are the first to target one conformational state of dynamin, inhibiting lipid-associated helical dynamin but not dynamin rings induced by self-assembly or SH3-domain-containing proteins.

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