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Michael R. Paddy

Researcher at University of California, Davis

Publications -  28
Citations -  2152

Michael R. Paddy is an academic researcher from University of California, Davis. The author has contributed to research in topics: Lamin & Nuclear pore. The author has an hindex of 21, co-authored 28 publications receiving 1889 citations. Previous affiliations of Michael R. Paddy include Max Planck Society & University of Florida.

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Interphase nuclear envelope lamins form a discontinuous network that interacts with only a fraction of the chromatin in the nuclear periphery

TL;DR: Using fluorescence microscopy to compare and quantitate the relationship between chromatin and the lamin network, it is found that although there is a strong tendency for the most peripheral chromatin to be positioned directly underneath a lamination fiber, only a small fraction of the chromatin in the nuclear periphery is sufficiently close to a lamin fiber to possibly be in direct contact.
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A Drosophila Tpr protein homolog is localized both in the extrachromosomal channel network and to nuclear pore complexes.

TL;DR: Structural, molecular, and biochemical characterizations of Bx34, a Drosophila melanogaster nuclear coiled-coil protein which is localized to extrachromosomal and extranucleolar spaces in the nuclear interior and which is homologous to the mammalian nuclear pore complex protein Tpr are reported.
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Drosophila nuclear lamin precursor Dm0 is translated from either of two developmentally regulated mRNA species apparently encoded by a single gene.

TL;DR: In vitro transcription of both full-length cDNA clones in a pT7 transcription vector followed by in vitro translation in wheat germ lysate suggests that both clones encode lamin Dm0, the polypeptide precursor of lamins Dm1 and Dm2.
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Characterization of Nuclear Polyadenylated RNA-binding Proteins in Saccharomyces cerevisiae

TL;DR: It is reported that Nab1p is identical to the Np13p/Nop3p protein recently implicated in both nucleocytoplasmic protein shuttling and pre-rRNA processing, and a new nuclear polyadenylated RNA-binding protein, Nab3p is characterized.