(Q57363455)

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Adsorption and aggregation of glycosylphosphatidyl inositol (GPI) anchored alkaline phosphatase on methylated glass surfaces studied by tapping mode atomic force microscopy

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scholarly article

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Adsorption and aggregation of glycosylphosphatidyl inositol (GPI) anchored alkaline phosphatase on methylated glass surfaces studied by tapping mode atomic force microscopy (English)

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author name string

J.P. Rieu

1

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F. Ronzon

2

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B. Roux

3

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publication date

March 2002

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Thin Solid Films

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406

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1-2

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241-249

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A new capacitive sensor for displacement measurement in a surface-force apparatus

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Mammalian GPI proteins: sorting, membrane residence and functions

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Functional rafts in cell membranes

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Detergent-insoluble glycosphingolipid/cholesterol-rich membrane domains, lipid rafts and caveolae (review).

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Crystal structure of alkaline phosphatase from human placenta at 1.8 A resolution. Implication for a substrate specificity

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High resolution AFM topographs of the Escherichia coli water channel aquaporin Z.

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The effect of deformation on the lateral resolution of atomic force microscopy

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Tapping-mode atomic force microscopy produces faithful high-resolution images of protein surfaces

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Detergent-mediated reconstitution of a glycosyl-phosphatidylinositol-protein into liposomes

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A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding

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Substrate preparation for reliable imaging of DNA molecules with the scanning force microscope.

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Correlation between surface morphology and surface forces of protein A adsorbed on mica

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Diffusion-limited aggregation: Connection to a free-boundary problem and lattice anisotropy

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Aggregation of HSA, IgG, and Fibrinogen on Methylated Silicon Surfaces

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Adsorption and Bioactivity of Protein A on Silicon Surfaces Studied by AFM and XPS

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Identifiers

10.1016/S0040-6090(02)00048-2

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