Annexin 2 belongs to the annexin family of proteins that bind to phospholipid membranes in
a Ca 2+-dependent manner. Here we show that, under mild acidic conditions, annexin 2 …

Revised Manuscript Received September 14, 19939 abstract: The modulating effect of the
variableN-terminus of annexins on the properties of these Ca2+-binding proteins was …

Annexins are a family of proteins generally described as Ca2+-dependent for phospholipid
binding. Yet, annexins have a wide variety of binding behaviors and conformational states …

Low-angle neutron solution scattering has been used to study the structure of annexin-V and
its interaction with small single-bilayer vesicles consisting of phosphatidylserine and …

Annexin A13 is considered the original progenitor of the 11 other members of vertebrate
annexins, a superfamily of calcium/phospholipid-binding proteins. It is highly tissue-specific …

The single tryptophan residue (Trp187) of human recombinant annexin V, containing 320
residues and 5328 atoms, was replaced with three different isosteric analogues where …

We have mutated the lysine 128 of domain II of annexin I, which flanks a putative calcium-
binding loop, into a glutamic acid residue. The properties of the mutated recombinant protein …

Annexins are homologous proteins that bind to membranes in a calcium dependent manner,
but for which precise physiological roles have yet to be defined. Most annexins are …

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 …

In 1993, Huber and co-workers published the structure of an N-terminally truncated version
of human annexin A1 lacking the first 32 amino acid residues (PDB code: 1AIN). In 2001, we …