https://ogma.newcastle.edu.au/vital/access/ /manager/Index ${session.getAttribute("locale")} 5 Pyrimidine-based inhibitors of dynamin I GTPase activity: competitive inhibition at the pleckstrin homology domain https://ogma.newcastle.edu.au/vital/access/ /manager/Repository/uon:32119 (CME) = 65.9 ± 7.7 to 3.7 ± 1.1 mM), which makes this series among the more potent inhibitors of dynamin and CME yet reported. In CME and growth inhibition cell-based assays, the data obtained was consistent with dynamin inhibition. CEREP ExpresS profiling identified off-target effects at the cholecystokinin, dopamine D₂, histamine H₁ and H₂, melanocortin, melatonin, muscarinic M₁ and M₃, neurokinin, opioid KOP and serotonin receptors.]]> Thu 03 May 2018 12:18:53 AEST ]]> Small molecule inhibitors of dynamin I GTPase activity: development of dimeric tyrphostins https://ogma.newcastle.edu.au/vital/access/ /manager/Repository/uon:2267 Sat 24 Mar 2018 08:26:55 AEDT ]]> Bacterial sliding clamp inhibitors that mimic the sequential binding mechanism of endogenous linear motifs. https://ogma.newcastle.edu.au/vital/access/ /manager/Repository/uon:28373 Escherichia coli sliding clamp occurs via a sequential mechanism that involves two subsites (I and II). Here, we report the development of small-molecule inhibitors that mimic this mechanism. The compounds contain tetrahydrocarbazole moieties as "anchors" to occupy subsite I. Functional groups appended at the tetrahydrocarbazole nitrogen bind to a channel gated by the side chain of M362 and lie at the edge of subsite II. One derivative induced the formation of a new binding pocket, termed subsite III, by rearrangement of a loop adjacent to subsite I. Discovery of the extended binding area will guide further inhibitor development.]]> Sat 24 Mar 2018 07:35:58 AEDT ]]>