Annexin A11 is one of the 12 vertebrate subfamilies in the annexin superfamily of
calcium/phospholipid-binding proteins, distinguishable by long, non-homologous N-termini …

The calcium binding properties of annexin I as observed by thermodynamic DSC studies
have been compared to the structural information obtained from X-ray investigation. The …

Annexins are a family of structurally related eukaryotic proteins that reversibly bind
membranes containing anionic phospholipids in a calcium-dependent manner.[1] More than …

The specific interaction of annexin A1 with phospholipid bilayers is scrutinized by means of
scanning force and fluorescence microscopy, quartz crystal microbalance, ellipsometry, and …

Isothermal titration calorimetry was used to characterize the binding of calcium ion (Ca 2+)
and phospholipid to the peripheral membrane-binding protein annexin a5. The phospholipid …

Three different systems are presented, exploring the adhesion of liposomes mediated by
electrostatic and lipid–protein interactions as well as molecular recognition of ligand …

The conformational rearrangements that take place after calcium binding in chicken annexin
A5 and a mutant lacking residues 3-10 were analyzed, in parallel with human annexin A5 …

Synaptotagmin I (Syt I) is a vesicle-localized protein implicated in sensing the calcium influx
that triggers fast synchronous release of neurotransmitter. How Syt I utilizes its two C2 …

The kinetics of annexin A1 binding to solid‐supported lipid bilayers consisting of 1‐palmitoyl‐
2‐oleoyl‐sn‐glycero‐3‐phosphocholine (POPC)/1‐palmitoyl‐2‐oleoyl‐sn‐glycero‐3 …

The von Willebrand factor (VWF) A1 and A3 domains are structurally isomorphic yet exhibit
distinct mechanisms of unfolding. The A1 domain, responsible for platelet adhesion to VWF …