Lysenin is a pore-forming toxin that binds to sphingomyelin in a distribution-dependent manner. Studies of this interaction revealed the heterogeneous organization of sphingomyelin in biomembranes while investigations with non-toxic lysenin helped elucidate the spatial and functional heterogeneity of lipid rafts. This chapter summarizes the characterization of lysenin and discusses the possible applications and limitations of this newly developed sphingomyelin probe. © Springer-Verlag Tokyo 2006. All rights reserved.
CITATION STYLE
Kobayashi, T., & Yamaji-Hasegawa, A. (2006). Lysenin: A new probe for sphingomyelin. In Sphingolipid Biology (pp. 475–482). Springer Japan. https://doi.org/10.1007/4-431-34200-1_37
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