During the past few years, the structural analysis of proteins and protein complexes by
chemical crosslinking and mass spectrometry has enjoyed increasing popularity. With this …

Annexin A2 is a pleiotropic calcium-and anionic phospholipid-binding protein that exists as
a monomer and as a heterotetrameric complex with the plasminogen receptor protein …

The four∼ 75-residue domains (repeats) that constitute the annexin core structure all
possess an identical five-α-helix bundle topology, but the physico-chemical properties of the …

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 …

Reaction-induced infrared difference spectroscopy (RIDS) has been used to investigate the
nature of interactions of human annexin A6 (ANXA6) with nucleotides. RIDS results for …

Abstract Annexin A2 (A2) is a member of the Annexin family, which contains Ca2+‐regulated
phospholipid‐binding proteins. Annexins associate with S100 proteins to form …

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 bind to biological membranes in a Ca2+-dependent
manner. Annexin-A6 (AnxA6) is unique in the annexin family as it consists of the repeat of …

Annexin A1 has been shown to cause membrane aggregation and fusion, yet the
mechanism of these activities is not clearly understood. In this work, molecular dynamics …

Annexins are peripheral membrane-binding proteins implicated in a number of membrane-
related events (for a review see refs.[1, 2]). Of particular interest within this family is annexin …