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by Bhatt, Deepak L and Steg, Philippe Gabriel and Steg, Philippe G and Mehta, Shamir and Mehta, Vimal and Mehta, Rajendra and Mehta, Shamir R and Mehta, Arvind and Leiter, Lawrence A and Simon, Tabassome and Fox, Kim and Held, Claes and Andersson, Marielle and Himmelmann, Anders and Ridderstråle, Wilhelm and Chen, Zhih-Cherng and Chen, Jersey and Song, Yang and Song, Zhifang and Diaz, Rafael and Goto, Shinya and James, Stefan K and Ray, Kausik K and Parkhomenko, Alexander and Parkhomenko, Oleksandr and Parkhomenko, Alexander N and Kosiborod, Mikhail N and Kosiborod, Mikhail and McGuire, Darren K and Harrington, Robert A and Santos, Queulla and Santos, Vladimir and Jain, Ashit and Lendel, Irina and Russo, Michael and Haught, W H and Bouza, Manuel and Gogia, Harinder and Banerjee, Supratim and Banerjee, Suvro and Banerjee, Subhash and Kichura, George and Kantaros, Louis and Padron, Francisco and Passi, Rakesh and Stone, Jay and Pursley, Michael and D'Urso, Michael and Gardner, Timothy and Bennett, James and Nour, Khaled and Saini, Satinder and Zhang, Ningru and Zhang, Aidong and Zhang, Wenwu and Zhang, Jian and Kumbhani, Dharam and Thomas, Dustin and Angiolillo, Dominick and Bertolet, Barry and Roman-Miranda, Amaury and Black, Robert and Manshadi, Ramin and Vaca, Carlos and Blanco, Antonio and Napoli, Mark and Brabham, David and Akyea-Djamson, Ayim and Desai, Pratik and Prasada, Sudhir and Khaira, Ajit and Forgosh, Leslie and Lieber, Ira and Umpierrez, Guillermo and Singal, Robert and Singal, Dinesh and Londono, Juan and Fraser, Neil and Ruiz, Jose and Vega, Damaris and Rodriguez, Lilia and Rodriguez, Aldo and Rodriguez, Manuel and Rodriguez, Mara and Rodriguez, Victor and Brown, Christopher and Syed, Faizullah and Syed, Mushtaq and Aggarwala, Guarav and Eaves, William and Foster, Michael and Foster, Malcolm and Gupta, Dinesh and Avino, David and Asfour, Wail and Tonnessen, Glen and Zhao, Xue-Qiao and Zhao, Qiang and Singh, Pradeep and Singh, Sanjay and ... and THEMIS Steering Committee and Investigators
The Lancet, ISSN 0140-6736, 09/2019, Volume 394, Issue 10204, pp. 1169 - 1180
Journal Article
Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, 12/2018, Volume 115, Issue 50, pp. 12733 - 12738
G protein-coupled receptor (GPCR) signaling from the extracellular orthosteric drug binding site across the cell membrane to the intracellular contact sites... 
Signaling | GPCR | Adenosine recepto | NMR spectroscopy | Dynamics | Biological Sciences | Physical Sciences | dynamics | signaling | adenosine receptor
Journal Article
Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, 9/2015, Volume 112, Issue 38, pp. 11852 - 11857
Journal Article
Structure, ISSN 0969-2126, 12/2016, Volume 24, Issue 12, p. 2190
Fluorine-19 nuclear magnetic resonance (NMR) was used to study conformational equilibria at the intracellular tips of helices VI and VII in a variant... 
Crystals | Fluorides | Research institutes | G proteins | Structure | Ethanolamines | Lysozyme | Membrane proteins | Protein binding
Journal Article
Proceedings of the National Academy of Sciences of the United States, ISSN 0027-8424, 12/2018, Volume 115, Issue 50, p. 12733
The human proteome contains 826 G protein-coupled receptors (GPCR), which control a wide array of key physiological functions, making them important drug... 
Physiological aspects | Nuclear magnetic resonance spectroscopy | Adenosine | Methods
Journal Article
Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, 12/2018, Volume 115, Issue 50, p. 12733
brane to intracellular binding sites for partners such as G proteins and arrestins. This signaling process is related to dynamic equilibria in conformational... 
Proteins | Signaling | Adenosine | Nuclear magnetic resonance--NMR | Spectrum analysis | Proteomics | Activation | Qualitative analysis | Receptor mechanisms | Intracellular | Binding sites
Journal Article
Structure, ISSN 0969-2126, 12/2016, Volume 24, Issue 12, pp. 2190 - 2197
Fluorine-19 nuclear magnetic resonance (NMR) was used to study conformational equilibria at the intracellular tips of helices VI and VII in a variant β... 
fusion protein | membrane proteins | β2-adrenergic receptor | protein dynamics | solution nuclear magnetic resonance | structural biology | solution NMR | integrative structural biology | 19F NMR spectroscopy | G-protein-coupled receptors
Journal Article
Structure (London, England : 1993), ISSN 0969-2126, 12/2016, Volume 24, Issue 12, pp. 2190 - 2197
Fluorine-19 nuclear magnetic resonance (NMR) was used to study conformational equilibria at the intracellular tips of helices VI and VII in a variant β... 
Protein Structure, Secondary | Signal Transduction | Humans | Models, Molecular | Nuclear Magnetic Resonance, Biomolecular | Crystallography, X-Ray | Muramidase - metabolism | Binding Sites | Arrestin - metabolism | Receptors, Adrenergic, beta-2 - metabolism | Receptors, Adrenergic, beta-2 - chemistry
Journal Article
Cell, ISSN 0092-8674, 01/2018, Volume 172, Issue 1-2, pp. 68 - 80.e12
Signaling across cellular membranes, the 826 human G protein-coupled receptors (GPCRs) govern a wide range of vital physiological processes, making GPCRs... 
G protein-coupled receptor | NMR | signaling | GPCR | membrane protein | nuclear magnetic resonance | allosteric modulation
Journal Article
Journal Article