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dc.contributor.authorSoo, Jianchowen
dc.contributor.authorZhang, Jingen
dc.contributor.authorHe, Qiyuanen
dc.contributor.authorAgarwal, Shuchien
dc.contributor.authorLi, Haien
dc.contributor.authorZhang, Huaen
dc.contributor.authorChen, Pengen
dc.identifier.citationSoo, J. C., Zhang, J., He, Q., Agarwal, S., Li, H., Zhang, H., et al. (2010). Surface immobilized cholera toxin B subunit (CTB) facilitates vesicle docking, trafficking and exocytosis. Integrative Biology, 2, 250–257.en
dc.description.abstractThe subunit B of cholera toxin (CTB), which specifically binds with ganglioside GM1 enriched in membrane lipid rafts, is known to interfere with multiple cell functions. However, the specific, stable and spatially defined membrane signaling induced by CTB binding is often difficult to investigate by applying CTB molecules in bulk solution due to quick internalization, elicited intracellular reactions, and homogeneous interaction with the entire cell membrane. Here, we interfaced the neuroendocrine PC12 cells with surface immobilized and patterned CTB molecules, and interrogated the effects of CTB binding on vesicular exocytosis using integrative single-cell study methods. It was discovered that CTB binding facilitates vesicle trafficking, docking and exocytosis in a cholesterol dependent manner. And these effects are probably attributable to the increased membrane GM1 and cholesterol, and enhanced Ca2+ signaling.en
dc.relation.ispartofseriesIntegrative biologyen
dc.rights© 2010 The Royal Society of Chemistry. This is the author created version of a work that has been peer reviewed and accepted for publication by Integrative Biology, The Royal Society of Chemistry. It incorporates referee’s comments but changes resulting from the publishing process, such as copyediting, structural formatting, may not be reflected in this document. The published version is available at:
dc.subjectDRNTU::Science::Biological sciencesen
dc.titleSurface immobilized cholera toxin B subunit (CTB) facilitates vesicle docking, trafficking and exocytosisen
dc.typeJournal Articleen
dc.contributor.schoolSchool of Materials Science & Engineeringen
dc.description.versionAccepted versionen
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