The hallmark of the annexin super family of proteins is Ca2+-dependent binding to
phospholipid bilayers, a property that resides in the conserved core domain of these …

Annexins are soluble proteins that can interact with membranes in a Ca2+-dependent
manner. Recent studies have shown that they can also undergo Ca2+-independent …

Annexins are abundant and ubiquitous proteins that bind, by their four structurally identical
domain cores, to phosphatidylserine-containing membranes in the presence of Ca 2+. Using …

Crystal structures of annexin V have shown up to 10 bound calcium ions in three different
types of binding sites, but previous work concluded that only one of these sites accounted for …

Annexins comprise a multigene family of Ca2+ and phospholipid-binding proteins. They
consist of a conserved C-terminal or core domain that confers Ca2+-dependent …

Annexins constitute a family of phospholipid-and Ca2+-binding proteins involved in a variety
of membrane-related processes. The property of several annexins, including annexin A5, to …

Annexin V belongs to a family of eukaryotic calcium-dependent membrane-binding proteins.
The calcium-binding sites at the annexin− membrane interface have been investigated in …

Annexins are soluble proteins that are best known for their ability to undergo reversible Ca
2+-dependent binding to the surface of phospholipid bilayers. Recent studies, however …

All annexins bind Ca 2+ and phospholipids, although individual annexins differ markedly in
their affinities for these ligands. Annexin I binds phosphatidylserine (PS) at lower [Ca 2+] …

Revised Manuscript Received August 24, 1994® abstract: The calcium-dependent
interaction of several annexins with membranes was studied. A novel technique was …