M
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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Journal ArticleDOI
Psychedelics Promote Structural and Functional Neural Plasticity
Calvin Ly,Alexandra C. Greb,Lindsay P. Cameron,Jonathan M. Wong,Eden V. Barragan,Paige C. Wilson,Kyle F. Burbach,Sina Soltanzadeh Zarandi,Alexander Sood,Michael R. Paddy,Whitney C. Duim,Megan Y. Dennis,A. Kimberley McAllister,Kassandra M. Ori-McKenney,John A. Gray,David E. Olson +15 more
TL;DR: It is reported that, like ketamine, serotonergic psychedelics are capable of robustly increasing neuritogenesis and/or spinogenesis both in vitro and in vivo.
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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.
Yosef Gruenbaum,Yosef Landesman,Barry Drees,John W. Bare,Harald Saumweber,Michael R. Paddy,John W. Sedat,David Smith,Bret M. Benton,Paul A. Fisher +9 more
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.