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 …

Site‐directed mutagenesis was employed to map and characterize Ca2+‐binding sites in
annexin II, a member of the annexin family of Ca2+–and phospholipid‐binding proteins …

Some annexins, including annexins I, II, IV, and VII, can promote membrane aggregation. To
identify amino acids involved in annexin I-mediated membrane aggregation, we generated …

Annexin II, a major cytoplasmic substrate of the src tyrosine kinase, is a member of the
annexin family of Ca2+/phospholipid-binding proteins. It is composed of a short N-terminal …

A wealth of high-resolution structural data has accumulated for soluble annexins, but only
limited information is available for the biologically important membrane-bound proteins. To …

Annexins comprise a family of proteins that is possibly relevant to in io functions such as the
formation of Ca2+ channels. The current work was undertaken to study the effect of annexin …

Revised Manuscript Received October 21, 1993* abstract: Phosphorylation of the N-terminal
tail by protein kinase C stronglyinhibits the ability of bovine or human annexin I to aggregate …

The behaviour of human annexin V in the presence of calcium was studied by NMR. We
observe the formation of well defined dimers, as well as a change in the local dynamics of …

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 conformational preferences and the solution structure of AnxIIN31, a peptide
corresponding to the full-length sequence (residues 1–31) of the human annexin II N …