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Cell signaling / Pharmacology / Protein families / G protein-coupled receptor / Receptor / Agonist / Ligand / Quenching / Biology / Signal transduction / Membrane biology


Agonist-induced conformational changes in the G-protein-coupling domain of the ␤2 adrenergic receptor Pejman Ghanouni*, Jacqueline J. Steenhuis*, David L. Farrens†, and Brian K. Kobilka*‡§ *Howard Hughes Medical I
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Document Date: 2009-12-04 19:10:05


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City

Portland / South Brunswick / Brunswick / FM / Metuchen / London / New York / /

Company

Spex Industries / Hubbell / TimeMaster Software / Bio-Rad / /

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Facility

Howard Hughes Medical Institute / Stanford University / Oregon Health Sciences University / Brian K. Kobilka*ठ*Howard Hughes Medical Institute / /

IndustryTerm

protease site / agonist-binding site / high energy state / important pharmaceutical target / cleavage site / sensory signaling systems / chemical reactivity measurements / fluorescein site / ligand-binding site / energy / /

Movie

A. D. / /

Organization

Oregon Health Sciences University / Agonist-Induced Movement of FM Bound / Stanford University Medical School / Division of Cardiovascular Medicine / Stanford University / Agonist-Induced Movement / Beckman Center / L. Farrens† / and Brian K. Kobilka*‡§ *Howard Hughes Medical Institute / Mathers Charitable Foundation / NHS / Howard Hughes Medical Institute / Stanford / Movement of FM Bound / /

Person

David L. Farrens / Jacqueline J. Steenhuis / Irache Visiers / Harel Weinstein / Roland Seifert / Dunham / Pejman Ghanouni / Brian K. Kobilka / Joseph Lakowicz / /

Position

Medical Scientist / Teller / luorescent reporter / T. D. / /

Product

potassium chloride / potassium iodide / /

ProvinceOrState

Oregon / California / New York / /

PublishedMedium

Molecular Biology / /

RadioStation

M FM / /

SportsLeague

Stanford University / /

Technology

Spectroscopy / CAT / /

URL

www.pnas.org兾cgi兾doi兾10.1073兾pnas.101126198 / /

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