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Rie Nygaard

Researcher at Columbia University

Publications -  30
Citations -  2430

Rie Nygaard is an academic researcher from Columbia University. The author has contributed to research in topics: G protein-coupled receptor & Allosteric regulation. The author has an hindex of 15, co-authored 24 publications receiving 2116 citations. Previous affiliations of Rie Nygaard include Bispebjerg Hospital & Stanford University.

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The Dynamic Process of β2-Adrenergic Receptor Activation

TL;DR: NMR spectroscopy is used to characterize the conformational dynamics of the transmembrane core of the β(2)-adrenergic receptor (β(2)AR), a prototypical GPCR, and shows that for β( 2)AR, unlike rhodopsin, an agonist alone does not stabilize a fully active conformation.
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Ligand-specific regulation of the extracellular surface of a G-protein-coupled receptor

TL;DR: NMR spectroscopy is used to demonstrate conformational coupling between the ECS and the orthosteric binding site, showing that drugs targeting this diverse surface could function as allosteric modulators with high subtype selectivity.
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Ligand binding and micro-switches in 7TM receptor structures

TL;DR: These structures demonstrate that the main ligand-binding pocket in 7TM receptors is like a funnel with a partial 'lid' in which extracellular loop 2b, in particular, functions as a gating element.

The Dynamic Process of b 2 -Adrenergic Receptor Activation

TL;DR: In this paper, NMR spectroscopy was used to characterize the conformational dynamics of the transmembrane core of the b2-adrenergic receptor (b2AR), a prototypical GPCR.
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A Conserved Aromatic Lock for the Tryptophan Rotameric Switch in TM-VI of Seven-transmembrane Receptors

TL;DR: It is concluded that Phe-V:13 can serve as an aromatic lock for the proposed active conformation of the Trp-VI:13 rotameric switch, being involved in the global movement of TM-V and TM-VI in 7TM receptor activation.