F
Frederick Lanni
Researcher at Carnegie Mellon University
Publications - 68
Citations - 5250
Frederick Lanni is an academic researcher from Carnegie Mellon University. The author has contributed to research in topics: Microscopy & Standing wave. The author has an hindex of 34, co-authored 66 publications receiving 5007 citations.
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Journal ArticleDOI
Enhancement of axial resolution in fluorescence microscopy by standing-wave excitation
TL;DR: In this article, standing waves formed by interference in laser illumination create an excitation field with closely spaced nodes and antinodes, allowing optical sectioning of the specimen at very high resolution.
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Hindered Diffusion of Inert Tracer Particles in the Cytoplasm of Mouse 3T3 Cells
TL;DR: The results reported here corroborate and extend the results of earlier experiments with fluorescein-labeled, size-fractionated dextran: diffusion of nonbinding particles in cytoplasm is hindered in a size-dependent manner, and suggest that, for native cy toplasmic particles whose smallest radial dimension approaches 260 A, size may be as important a determinant of cytop lasmic diffusibility as binding specificity.
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Experimental test of an analytical model of aberration in an oil-immersion objective lens used in three-dimensional light microscopy.
TL;DR: In this article, a model of the three-dimensional imaging properties of a fluorescence light microscope subject to aberration is presented, which can be used to understand and compensate for aberration introduced to a microscope system under nondesign optical conditions so that both confocal laser scanning microscopy and optical serial sectioning microscopy can be optimized.
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Probing the structure of cytoplasm.
TL;DR: The combined fluorescence recovery after photobleaching and imaging data suggest that the average pore size of the meshwork is in the range of 300 to 400 A, but may be as small as 200 A in some cytoplasmic domains.
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GM130 and GRASP65-dependent lateral cisternal fusion allows uniform Golgi-enzyme distribution.
Manojkumar A. Puthenveedu,Collin Bachert,Sapna Puri,Sapna Puri,Frederick Lanni,Adam D. Linstedt +5 more
TL;DR: It is demonstrated that ribbon formation is mediated by specific membrane-fusion events that occur during Golgi assembly, and require the Golgi proteins GM130 and GRASP65.