Nagae, Masamichi <br/><br/>
Structure of the F-spondin reeler domain reveals a unique beta-sandwich fold with a deformable disulfide-bonded loop.  [electronic resource] 

 -  Acta crystallographica. Section D, Biological crystallography  Nov 2008 
 - 1138-45 p.  digital 
<br/><br/> Publication Type: Journal Article; Research Support, Non-U.S. Gov't 
<br/><br/><label>ISSN: </label>1399-0047 
<br/><br/><label>Standard No.: </label>10.1107/S0907444908028308  doi 
<br/><br/><label>Subjects--Topical Terms: </label><br/>Amino Acid Sequence<br/>Animals<br/>Cell Adhesion Molecules, Neuronal--chemistry<br/>Crystallization<br/>Disulfides--chemistry<br/>Extracellular Matrix--metabolism<br/>Extracellular Matrix Proteins--chemistry<br/>Humans<br/>Inverted Repeat Sequences--genetics<br/>Molecular Sequence Data<br/>Nerve Tissue Proteins--chemistry<br/>Protein Structure, Secondary--genetics<br/>Protein Structure, Tertiary--genetics<br/>Reelin Protein<br/>Sequence Alignment<br/>Serine Endopeptidases--chemistry<br/>Transgenes--genetics