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• W4282978312 endingPage "102401" @default.
• W4282978312 startingPage "102401" @default.
• W4282978312 abstract "Deployed by both pathogenic bacteria and host immune systems, pore-forming proteins rupture target membranes and can serve as conduits for effector proteins. Understanding how these proteins work relies on capturing assembly intermediates. Advances in cryoEM allowing in silico purification of heterogeneous assemblies has led to new insights into two main classes of pore-forming proteins: membrane attack complex perforin (MACPF) proteins and binary toxins. The structure of an immune activation complex, sMAC, shows how pores form by sequential templating and insertion of β-hairpins. CryoEM structures of bacterial binary toxins present a series of transitions along the pore formation pathway and reveal a general mechanism of effector protein translocation. Future developments in time-resolved cryoEM could capture and place short-lived states along the trajectory of pore-formation." @default.
• W4282978312 created "2022-06-17" @default.
• W4282978312 creator A5066985367 @default.
• W4282978312 creator A5077066530 @default.
• W4282978312 date "2022-08-01" @default.
• W4282978312 modified "2023-09-27" @default.
• W4282978312 title "Capturing pore-forming intermediates of MACPF and binary toxin assemblies by cryoEM" @default.
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• W4282978312 doi "https://doi.org/10.1016/j.sbi.2022.102401" @default.
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