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Sudha K. Shenoy

Researcher at Duke University

Publications -  86
Citations -  13174

Sudha K. Shenoy is an academic researcher from Duke University. The author has contributed to research in topics: Arrestin & G protein-coupled receptor. The author has an hindex of 41, co-authored 82 publications receiving 12132 citations. Previous affiliations of Sudha K. Shenoy include Oklahoma State University–Stillwater & Howard Hughes Medical Institute.

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Transduction of receptor signals by beta-arrestins.

TL;DR: Another previously unappreciated strategy used by the receptors to regulate intracellular signaling pathways is indicated, which regulates aspects of cell motility, chemotaxis, apoptosis, and likely other cellular functions through a rapidly expanding list of signaling pathways.
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β-Arrestins and Cell Signaling

TL;DR: The signaling capacities of these versatile adapter molecules are reviewed and the possible implications for cellular processes such as chemotaxis and apoptosis are discussed.
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Regulation of Receptor Fate by Ubiquitination of Activated β2-Adrenergic Receptor and β-Arrestin

TL;DR: It is indicated that ubiquitination of the receptor and of β-arrestin have distinct and obligatory roles in the trafficking and degradation of this prototypic GPCR.
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β-Arrestin-dependent, G Protein-independent ERK1/2 Activation by the β2 Adrenergic Receptor

TL;DR: It is demonstrated that the β2AR can signal to ERK via a GRK5/6-β-arrestin-dependent pathway, which is independent of G protein coupling, and GRK2, membrane translocation of which requires Gβγ release upon G protein activation, was ineffective unless it was constitutively targeted to the plasma membrane by a prenylation signal.
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Independent β-arrestin 2 and G protein-mediated pathways for angiotensin II activation of extracellular signal-regulated kinases 1 and 2

TL;DR: These findings imply the existence of independent G protein- and β-arrestin 2-mediated pathways leading to ERK1/2 activation and theexistence of distinct “active” conformations of a seven-membrane-spanning receptor coupled to each.