Limited proteolysis of the core domain of the 36‐kDa protein p36 by trypsin gives a first
insight into the structural organization of the four annexin repeats. Trypsin opens only a …

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 …

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 …

Revised Manuscript Received April 5, 1990 abstract: The existence of a single tryptophan
residue in the protein p36, a member of a recently characterized family of Ca2+ binding …

Abstract cDNA coding for N‐terminally truncated human annexin I, a member of the family of
Ca2+‐dependent phospholipid binding proteins, has been cloned and expressed in …

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 …

Annexin A9 is a novel member of the annexin family of Ca2+ and phospholipid binding
proteins which has so far only been identified in EST data bases and whose deduced …

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+] …

All the functions of annexins in vitro as well as in vivo are mediated and probably regulated
by calcium. We have used recombinant annexin I, synthesized by Escherichia coli, and we …

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 …