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Cryo-EM structure of human rhodopsin bound to an inhibitory G protein

Nature (London), 2018-06, Vol.558 (7711), p.553-558

2018

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Mechanistic insights into allosteric regulation of the A2A adenosine G protein-coupled receptor by physiological cations

Nature communications, 2018-04, Vol.9 (1), p.1-13, Article 1372

2018

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

Nature, 2008-09, Vol.455 (7212), p.497-502

2008

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High-resolution distance mapping in rhodopsin reveals the pattern of helix movement due to activation

Proceedings of the National Academy of Sciences - PNAS, 2008-05, Vol.105 (21), p.7439-7444

2008

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Crystal structure of pre-activated arrestin p44

Nature (London), 2013-05, Vol.497 (7447), p.142-146

2013

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A ligand channel through the G protein coupled receptor opsin

PloS one, 2009-02, Vol.4 (2), p.e4382-e4382

2009

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Crystal structure of metarhodopsin II

Nature (London), 2011-03, Vol.471 (7340), p.651-655

2011

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Monomeric G Protein-Coupled Receptor Rhodopsin in Solution Activates Its G Protein Transducin at the Diffusion Limit

Proceedings of the National Academy of Sciences - PNAS, 2007-06, Vol.104 (26), p.10859-10864

2007

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Structure of the glucagon receptor in complex with a glucagon analogue

Nature (London), 2018-01, Vol.553 (7686), p.106-110

2018

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Stationary Phase EPR Spectroscopy for Monitoring Membrane Protein Refolding by Conformational Response

Analytical chemistry (Washington), 2019-01, Vol.91 (1), p.1071-1079

2019

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Sequence of Late Molecular Events in the Activation of Rhodopsin

Proceedings of the National Academy of Sciences - PNAS, 2007-12, Vol.104 (51), p.20290-20295

2007

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Effect of channel mutations on the uptake and release of the retinal ligand in opsin

Proceedings of the National Academy of Sciences - PNAS, 2012-04, Vol.109 (14), p.5247-5252

2012

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Conformation of receptor-bound visual arrestin

Proceedings of the National Academy of Sciences - PNAS, 2012-11, Vol.109 (45), p.18407-18412

2012

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High-throughput in situ X-ray screening of and data collection from protein crystals at room temperature and under cryogenic conditions

Nature protocols, 2018-02, Vol.13 (2), p.260-292

2018

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Engineering of an artificial light-modulated potassium channel

PloS one, 2012-08, Vol.7 (8), p.e43766-e43766

2012

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

Nature (London), 2015-07, Vol.523 (7562), p.561-567

2015

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Activation of the A2A adenosine G-protein-coupled receptor by conformational selection

Nature (London), 2016-05, Vol.533 (7602), p.265-268

2016

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Structural and Kinetic Modeling of an Activating Helix Switch in the Rhodopsin-Transducin Interface

Proceedings of the National Academy of Sciences - PNAS, 2009-06, Vol.106 (26), p.10660-10665

2009

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Ion channel in the spotlight

Nature (London), 2012-02, Vol.482 (7385), p.318-319

2012

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X-ray transparent microfluidic chips for high-throughput screening and optimization of in meso membrane protein crystallization

Biomicrofluidics, 2017-03, Vol.11 (2), p.024118-024118

2017

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Signal Transfer from Rhodopsin to the G-Protein: Evidence for a Two-Site Sequential Fit Mechanism

Proceedings of the National Academy of Sciences - PNAS, 1999-04, Vol.96 (9), p.4898-4903

1999

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Synthesis and Spectroscopic Characterization of Photo-affinity Peptide Ligands to Study Rhodopsin-G Protein Interaction

Photochemistry and photobiology, 2008-07, Vol.84 (4), p.831-838

2008

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Activation of the A.sub.2A adenosine G-protein-coupled receptor by conformational selection

Nature (London), 2016-05, Vol.533 (7602), p.265

2016

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Ion channel in the spotlight: when expressed in neurons, channelrhodopsin proteins allow the cells' electrical activity to be controlled by light. The structure of one such protein will guide efforts to make better tools for controlling neurons.(STRUCTURAL BIOLOGY)

Nature (London), 2012-02, Vol.482 (7385), p.318

2012

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Cryo-EM structure of human rhodopsin bound to an inhibitory G protein

Mechanistic insights into allosteric regulation of the A2A adenosine G protein-coupled receptor by physiological cations

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

High-resolution distance mapping in rhodopsin reveals the pattern of helix movement due to activation

Crystal structure of pre-activated arrestin p44

A ligand channel through the G protein coupled receptor opsin

Crystal structure of metarhodopsin II

Monomeric G Protein-Coupled Receptor Rhodopsin in Solution Activates Its G Protein Transducin at the Diffusion Limit

Structure of the glucagon receptor in complex with a glucagon analogue

Broadly neutralizing humanized SARS-CoV-2 antibody binds to a conserved epitope on Spike and provides antiviral protection through inhalation-based delivery in non-human primates

Stationary Phase EPR Spectroscopy for Monitoring Membrane Protein Refolding by Conformational Response

Sequence of Late Molecular Events in the Activation of Rhodopsin

Effect of channel mutations on the uptake and release of the retinal ligand in opsin

Conformation of receptor-bound visual arrestin

High-throughput in situ X-ray screening of and data collection from protein crystals at room temperature and under cryogenic conditions

Engineering of an artificial light-modulated potassium channel

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

Activation of the A2A adenosine G-protein-coupled receptor by conformational selection

Structural and Kinetic Modeling of an Activating Helix Switch in the Rhodopsin-Transducin Interface

Ion channel in the spotlight

X-ray transparent microfluidic chips for high-throughput screening and optimization of in meso membrane protein crystallization

Signal Transfer from Rhodopsin to the G-Protein: Evidence for a Two-Site Sequential Fit Mechanism

Synthesis and Spectroscopic Characterization of Photo-affinity Peptide Ligands to Study Rhodopsin-G Protein Interaction

Activation of the A.sub.2A adenosine G-protein-coupled receptor by conformational selection

Ion channel in the spotlight: when expressed in neurons, channelrhodopsin proteins allow the cells' electrical activity to be controlled by light. The structure of one such protein will guide efforts to make better tools for controlling neurons.(STRUCTURAL BIOLOGY)

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