The arrestin-1 finger loop interacts with two distinct conformations of active rhodopsin.

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The arrestin-1 finger loop interacts with two distinct conformations of active rhodopsin.

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2018 nî lūn-bûn

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2018年の論文

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2018年学术文章

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The arrestin-1 finger loop interacts with two distinct conformations of active rhodopsin.

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The arrestin-1 finger loop interacts with two distinct conformations of active rhodopsin.

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The arrestin-1 finger loop interacts with two distinct conformations of active rhodopsin.

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The arrestin-1 finger loop interacts with two distinct conformations of active rhodopsin.

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The arrestin-1 finger loop interacts with two distinct conformations of active rhodopsin.

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The arrestin-1 finger loop interacts with two distinct conformations of active rhodopsin.

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P1476

The arrestin-1 finger loop interacts with two distinct conformations of active rhodopsin.

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P2093

Franz J Bartl

http://www.w3.org/2001/XMLSchema#string

Klaus Peter Hofmann

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Matthias Elgeti

http://www.w3.org/2001/XMLSchema#string

Michal Szczepek

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Peter W Hildebrand

http://www.w3.org/2001/XMLSchema#string

Roman Kazmin

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P2860

Rhodopsin mutations responsible for autosomal dominant retinitis pigmentosa. Clustering of functional classes along the polypeptide chain

Crystal structure of the β2 adrenergic receptor-Gs protein complex

Crystal structure of rhodopsin bound to arrestin by femtosecond X-ray laser

Crystal structure of the ligand-free G-protein-coupled receptor opsin

Crystal structure of opsin in its G-protein-interacting conformation

Stabilized G protein binding site in the structure of constitutively active metarhodopsin-II

GPCR-G Protein-β-Arrestin Super-Complex Mediates Sustained G Protein Signaling

Conformational equilibria of light-activated rhodopsin in nanodiscs.

Divergent transducer-specific molecular efficacies generate biased agonism at a G protein-coupled receptor (GPCR)

Highly conserved tyrosine stabilizes the active state of rhodopsin.

P31

scholarly article

P356

10.1074/JBC.M117.817890

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P407

English

P50

Alexander S Rose

Patrick Scheerer

P577

2018-01-23T00:00:00Z

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P698

29363577

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P932

5868258

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