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Sec1/Munc18 (SM) proteins shield SNARE complexes from NSF/Sec18-mediated disassembly through cooperative binding interactions with SNARE complexes and the universal co-chaperone α-SNAP/Sec17.

The ability of lipid nanodiscs to trap different types of amyloid intermediates, as successfully demonstrated in this study for human-IAPP, could become one of the most powerful approaches to dissect the complicated misfolding pathways of protein aggregation.

Naturally-occurring v-SNARE TMD variants differentially regulate fusion pore dynamics and cooperate with phospholipids in supporting membrane curvature at the fusion pore neck.

Trapping of the cell envelope proteome into water-soluble peptidisc library allows high-throughput definition of the membrane protein interactome.

Determination of a model of mitochondrial protein import elucidated using a high-resolution transport assay and kinetic modelling.

Disassembly of the HIV-1 capsid is a catastrophic process, whereby initiation and propagation can be controlled independently by molecules that bind to different features of the capsid lattice.

Complexin, in conjunction with Synaptotagmin, clamps the SNARE-assembly process under resting conditions and promote vesicle fusion in response to calcium signal.

Long-lived intermediate states formed by glycoprotein catalysts are an essential part of the process used by influenza virus particles to infect cells.

The mechanism of membrane-fusion catalysis in influenza viral infection of target cells is robust against the presence of a large fraction of non-productive viral fusion proteins.

Eugenol has the potential as a novel exercise mimetic, and TRPV1 may represent a promising target for the development of exercise mimetics.