Characterization of caveolin-rich membrane domains isolated from an endothelial-rich source: implications for human disease (original) (raw)
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Trends in Cell Biology, 1994
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Caveolin-2 Localizes to the Golgi Complex but Redistributes to Plasma Membrane, Caveolae, and Rafts when Co-expressed with Caveolin-1
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Caveolae Are Highly Immobile Plasma Membrane Microdomains, Which Are not Involved in Constitutive Endocytic Trafficking
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A Role for the Caveolin Scaffolding Domain in Mediating the Membrane Attachment of Caveolin-1. THE CAVEOLIN SCAFFOLDING DOMAIN IS BOTH NECESSARY AND SUFFICIENT FOR MEMBRANE BINDING IN VITRO
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Signal transducing molecules and glycosyl-phosphatidylinositol-linked proteins form a caveolin-rich insoluble complex in MDCK cells
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Co-purification and Direct Interaction of Ras with Caveolin, an Integral Membrane Protein of Caveolae Microdomains
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Endothelial-specific expression of caveolin-1 impairs microvascular permeability and angiogenesis
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Phosphatidylserine dictates the assembly and dynamics of caveolae in the plasma membrane
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