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Nicholas S. Duesbery

Researcher at Van Andel Institute

Publications -  63
Citations -  3248

Nicholas S. Duesbery is an academic researcher from Van Andel Institute. The author has contributed to research in topics: Protein kinase A & Anthrax toxin. The author has an hindex of 26, co-authored 63 publications receiving 3103 citations. Previous affiliations of Nicholas S. Duesbery include Harvard University & Duke University.

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Proteolytic Inactivation of MAP-Kinase-Kinase by Anthrax Lethal Factor

TL;DR: It is shown that LF is a protease that cleaves the amino terminus of mitogen-activated protein kinase kinases 1 and 2 and that this cleavage inactivates MAPKK1 and inhibits the MAPK signal transduction pathway.
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Cytoplasmic control of nuclear behavior during meiotic maturation of frog oocytes

TL;DR: The experiments that led to the discoveries of the meiotic regulatory activities maturation promoting factor and cytostatic factor are reviewed and their relation to current knowledge of the biochemistry of oocyte maturation is discussed.
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Inhibition of MAPK kinase signaling pathways suppressed renal cell carcinoma growth and angiogenesis in vivo.

TL;DR: The mitogen-activated protein kinase (MAPK) signaling pathways play essential roles in cell proliferation and differentiation as discussed by the authors, and the role of MAPK signaling pathways in regulating the proliferation and survival of RCC cells.
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Apoptosis and melanogenesis in human melanoma cells induced by anthrax lethal factor inactivation of mitogen-activated protein kinase kinase

TL;DR: In vivo treatment of human melanoma xenograft tumors in athymic nude mice with LeTx results in significant or complete tumor regression without apparent side effects, suggesting that inhibiting the MAPK signaling pathway may be a useful strategy for treating melanoma.
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Anthrax lethal factor proteolysis and inactivation of MAPK kinase.

TL;DR: By means of deletion mutant analysis and site-directed mutagenesis, an LFIR (LF interacting region) is identified in the COOH-terminal kinase domain of MEK1 adjacent to the proline-rich region, which is essential for LF-mediated proteolysis ofMEK.