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Nicole S. Schonenbach

University of California, Santa Barbara

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Author response: Homo-oligomerization of the human adenosine A2A receptor is driven by the intrinsically disordered C-terminus

2021 eLife
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Homo-oligomerization of the human adenosine A2A receptor is driven by the intrinsically disordered C-terminus

2021 eLife
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Oligomerization of the Human Adenosine A2A Receptor Is Driven by the Intrinsically Disordered C-Terminus

2020 bioRxiv
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Human Adenosine A2AR Dimerization is Driven by a C-terminal Motif

2020 Biophysical Journal
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Dimerization of Human Adenosine A2AReceptor - Impact of the C-Terminus

2019 Biophysical Journal
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Adenosine A2a receptors form distinct oligomers in protein detergent complexes

2016 FEBS Letters
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Functional Consequences of the Oligomeric Assembly of Proteorhodopsin

2015 Journal of Molecular Biology
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Tuning Function of the Light-Driven Proteorhodopsin Proton Pump by Formation of Oligomeric and Surfactant-Based Synthetic Complexes

2014 Biophysical Journal
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