Annexins constitute an evolutionary conserved multigene protein superfamily characterized
by their ability to interact with biological membranes in a calcium dependent manner. They …

Site-directed spin labeling has become a popular biophysical tool for the characterization of
protein structure, dynamics and conformational change. This method is well suited and …

Plant annexins are ubiquitous, soluble proteins capable of Ca2+-dependent and Ca2+-
independent binding to endomembranes and the plasma membrane. Some members of this …

Annexins are small proteins capable of membrane attachment or insertion. Animal annexins
can form Ca 2+-permeable conductances in planar lipid bilayers or vesicles. Some have …

Preferential binding of proteins on curved membranes (membrane curvature sensing) is
increasingly emerging as a general mechanism whereby cells may effect protein localization …

Annexins are a family of structurally related, Ca 2+-sensitive proteins that bind to negatively
charged phospholipids and establish specific interactions with other lipids and lipid …

The spatiotemporal regulation of calcium (Ca2+) storage in late endosomes (LE) and
lysosomes (Lys) is increasingly recognized to influence a variety of membrane trafficking …

Annexins are soluble proteins that undergo conditional association or insertion into
membranes. Plants contain several isoforms, each of which may be capable of supporting …

Initially viewed as innovative carriers for biomedical applications, with unique photophysical
properties and great versatility to be decorated at their surface with suitable molecules …

Site-directed spin labeling and electron paramagnetic resonance spectroscopy have
recently experienced an outburst of multiple applications in protein science. Numerous …