The transmembrane domains of fusion proteins are known to be important for their fusogenic
activity. In an effort to systematically investigate the structure/function relationships of …

Fusion of biological membranes is mediated by distinct integral membrane proteins, eg,
soluble N-ethylmaleimide-sensitive factor attachment protein receptors and viral fusion …

LV-peptides mimic the in vitro fusogenicity of synthetic fusion protein transmembrane
domains. The original versions of these peptides consist of a variable hydrophobic core …

LV-peptides were designed as membrane-spanning low-complexity model structures that
mimic fusion protein transmembrane domains. These peptides harbor a hydrophobic core …

Membrane fusion requires restructuring of lipid bilayers mediated by fusogenic membrane
proteins. Peptides that correspond to natural transmembrane sequences or that have been …

Membrane fusion plays a lead role in the transport of vesicles, neurotransmission,
mitochondrial dynamics, and viral infection. There are fusion proteins that catalyze and …

Membrane fusion is ubiquitous in life. Fusion of biological membranes is mediated by
specialized fusion proteins anchored to the bilayers destined to fuse. Here we describe …

Membrane fusion, one of the most essential processes in the life of eukaryotes, occurs when
two separate lipid bilayers merge into a continuous bilayer and internal contents of two …

Biological membrane fusion is driven by different types of molecular fusion machines. Most
of these proteins are membrane-anchored by single transmembrane domains. SNARE …

It has been suggested that lipids translocate between the outer and inner leaflets of fusing
membranes, or flip–flop, to facilitate changes in bilayer leaflet areas at various stages of …