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High-throughput characterization of 309 photocrosslinker-bearing ASIC1a variants maps residues critical for channel function and pharmacology
View ORCID ProfileNina Braun, Søren Friis, Christian Ihling, View ORCID ProfileAndrea Sinz, View ORCID ProfileJacob Andersen, View ORCID ProfileStephan A. Pless
doi: https://doi.org/10.1101/2020.11.24.392498
Nina Braun
1Department of Drug Design and Pharmacology, University of Copenhagen, Copenhagen, Denmark
Søren Friis
2Nanion Technologies GmbH, Munich, Germany
Christian Ihling
3Department of Pharmaceutical Chemistry & Bioanalytics, Institute of Pharmacy, Charles Tanford Protein Center, Martin Luther University Halle-Wittenberg, Halle (Saale), Germany
Andrea Sinz
3Department of Pharmaceutical Chemistry & Bioanalytics, Institute of Pharmacy, Charles Tanford Protein Center, Martin Luther University Halle-Wittenberg, Halle (Saale), Germany
Jacob Andersen
1Department of Drug Design and Pharmacology, University of Copenhagen, Copenhagen, Denmark
Stephan A. Pless
1Department of Drug Design and Pharmacology, University of Copenhagen, Copenhagen, Denmark
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Posted December 04, 2020.
High-throughput characterization of 309 photocrosslinker-bearing ASIC1a variants maps residues critical for channel function and pharmacology
Nina Braun, Søren Friis, Christian Ihling, Andrea Sinz, Jacob Andersen, Stephan A. Pless
bioRxiv 2020.11.24.392498; doi: https://doi.org/10.1101/2020.11.24.392498
High-throughput characterization of 309 photocrosslinker-bearing ASIC1a variants maps residues critical for channel function and pharmacology
Nina Braun, Søren Friis, Christian Ihling, Andrea Sinz, Jacob Andersen, Stephan A. Pless
bioRxiv 2020.11.24.392498; doi: https://doi.org/10.1101/2020.11.24.392498
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