Rigorous assays of membrane fusion show that a distinct tethering step is required for lumenal compartment mixing in a manner that extends beyond simply increasing the amount of total trans-SNARE complex.

Computational modeling of a dynamin-constricted membrane neck can rank proposed shape changes of the helical scaffold in terms of their fission aptitude and elucidate the associated pathways.

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.

The mechanism triggering HBV membrane fusion involves ERp57, a cellular protein disulfide isomerase, and ultimately leads to the exposition of a fusion peptide that was identified in the pre-S1 determinant.

The West Nile Virus envelope protein catalyzes membrane fusion through low-pH induced conformational rearrangement, with a rate determined by the formation of two trimeric complexes at the contact zone between the virus and target membrane.

The structure of the yeast HOPS tethering complex suggests how this large complex may catalyze fusion by tethering Rab-decorated membranes and promoting the assembly of SNAREs.

The BAR protein endophilin spaces out turns of the dynamin helix, blocking its active conformational change and membrane fission.

When the Ca²⁺-binding loops of the C2B domain insert into a membrane, interactions with a phospholipid and the SNARE complex allow synaptotagmin-1 to bend the membrane.

Structural flexibility of the synaptobrevin-2 transmembrane domain promotes membrane fusion.