@article{oai:teapot.lib.ocha.ac.jp:00043224,
 author = {KUROIWA, Sachiko and TOI, Sayo and KOJIMA-AIKAWA, Kyoko},
 issue = {特別号},
 journal = {お茶の水女子大学自然科学報告},
 month = {Sep},
 note = {紀要論文, Annexin (ANX) is a family of Ca2+-dependent membrane/lipid binding proteins; altogether 12 types (ANXA1-A11 and A13) have been identified in the mammalian genome. Some of these are important regulators of the cell membrane organization, trafficking, repair, etc. Among them, ANXA9 is the only ANX that does not have the type II Ca2+ binding site. ANXs commonly bind to phosphatidylserine (one of the plasma membrane components), via the type II Ca2+ binding sites but does not bind to cholesterol. Therefore, ANXA9 appears to have different lipid binding properties and biological functions from other ANXs. In this study, we examined the binding ability of recombinant ANXA9 to cholesterol and its derivatives via the solid-phase assay and characterized the molecular structure of ANXA9 by circular dichroism spectrometry, by determining amino acid sequence motifs, and molecular modeling.},
 pages = {58--66},
 title = {Lipid Binding Properties of Annexin A9},
 volume = {71},
 year = {2020}
}