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Nicole C. McKnight

Researcher at Icahn School of Medicine at Mount Sinai

Publications -  14
Citations -  1137

Nicole C. McKnight is an academic researcher from Icahn School of Medicine at Mount Sinai. The author has contributed to research in topics: Autophagy & LNCaP. The author has an hindex of 11, co-authored 14 publications receiving 1039 citations. Previous affiliations of Nicole C. McKnight include London Research Institute & Beth Israel Deaconess Medical Center.

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Kinase-inactivated ULK proteins inhibit autophagy via their conserved c-terminal domains using an Atg13-independent mechanism

TL;DR: It is demonstrated that the dominant-negative activity of kinase-dead mutants requires a 7-residue motif within the CTD, which leads to a model in which the functions of ULK1 and ULK2 are controlled by autophosphorylation and conformational changes involving exposure of theCTD.
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SOX9 is expressed in normal prostate basal cells and regulates androgen receptor expression in prostate cancer cells.

TL;DR: The results indicate that SOX9 in prostate basal cells supports the development and maintenance of the luminal epithelium and that a subset of prostate cancer cells may escape basal cell requirements throughSOX9 expression.
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Genome-wide siRNA screen reveals amino acid starvation-induced autophagy requires SCOC and WAC.

TL;DR: The identification of these novel regulatory proteins with diverse functions in autophagy contributes towards a fuller understanding of autophagosome formation.
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Beclin 1 Is Required for Neuron Viability and Regulates Endosome Pathways via the UVRAG-VPS34 Complex

TL;DR: This study reveals the essential role for beclin 1 in neuron survival involving multiple membrane trafficking pathways including endocytosis and autophagy, and suggests that the UVRAG-beclin 2 interaction underlies becl in 1's function in endocyTosis.
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Beclin 1, an Essential Component and Master Regulator of PI3K-III in Health and Disease.

TL;DR: Beclin 1 seems to function as an adaptor for recruiting multiple proteins that modulate VPS34, enabling the recruitment of a number of autophagy proteins involved in the nucleation of the autophagosome.