J
Jeffrey S. Nye
Researcher at Johnson & Johnson
Publications - 55
Citations - 6946
Jeffrey S. Nye is an academic researcher from Johnson & Johnson. The author has contributed to research in topics: Notch signaling pathway & Notch proteins. The author has an hindex of 32, co-authored 55 publications receiving 6706 citations. Previous affiliations of Jeffrey S. Nye include Johns Hopkins University & Johns Hopkins University School of Medicine.
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Journal ArticleDOI
aph-1 and pen-2 Are Required for Notch Pathway Signaling, γ-Secretase Cleavage of βAPP, and Presenilin Protein Accumulation
Ross Francis,Garth Joseph Mcgrath,Jianhuan Zhang,David A. Ruddy,Mary Sym,Javier Apfeld,Monique Nicoll,Mark E. Maxwell,Bing Hai,Michael C. Ellis,Annette L. Parks,Wei Xu,Jinhe Li,Mark E. Gurney,Richard L. Myers,Carol S. Himes,Ronald Hiebsch,Cara L. Ruble,Jeffrey S. Nye,Daniel Tim Curtis +19 more
TL;DR: RNAi-mediated inactivation of aph-1, pen-2, or nicastrin in cultured Drosophila cells reduces gamma-secretase cleavage of betaAPP and Notch substrates and reduces the levels of processed presenilin.
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Radial Glial Identity Is Promoted by Notch1 Signaling in the Murine Forebrain
TL;DR: It is suggested that Notch1 promotes radial glial identity during embryogenesis, and that radial glia may be lineally related to stem cells in the adult nervous system.
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Notch pathway molecules are essential for the maintenance, but not the generation, of mammalian neural stem cells.
Seiji Hitoshi,Tania O. Alexson,Vincent Tropepe,Dorit B. Donoviel,Andrew J. Elia,Jeffrey S. Nye,Ronald A. Conlon,Tak W. Mak,Alan Bernstein,Derek van der Kooy +9 more
TL;DR: Both neuronal and glial differentiation in vitro were enhanced by attenuation of Notch signaling and suppressed by expressing an active form of NotCh1, consistent with a role for NotCh signaling in the maintenance of the neural stem cell, and inconsistent with a roles in a neuronal/glial fate switch.
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The intracellular domain of mouse Notch: a constitutively activated repressor of myogenesis directed at the basic helix-loop-helix region of MyoD
TL;DR: It is shown that ectopic expression of the intracellular domain of mNotch (mNotchIC) functions as a constitutively activated repressor of myogenesis both in cultured cells and in frog embryos.
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Signal transduction by activated mNotch: importance of proteolytic processing and its regulation by the extracellular domain
TL;DR: It is demonstrated that a mNotch1 mutant protein that lacks its extracellular domain but retains its membrane-spanning region becomes proteolytically processed on its intracellular surface and, as a result, the activated intrACEllular domain (mNotchIC) is released and can move to the nucleus.