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View article: Reviewer #2 (Public Review): Folding of Prestin’s Anion-Binding Site and the Mechanism of Outer Hair Cell Electromotility
Reviewer #2 (Public Review): Folding of Prestin’s Anion-Binding Site and the Mechanism of Outer Hair Cell Electromotility Open
Prestin responds to transmembrane voltage fluctuations by changing its cross-sectional area, a process underlying the electromotility of outer hair cells and cochlear amplification. Prestin belongs to the SLC26 family of anion transporters…
View article: Reviewer #1 (Public Review): Folding of Prestin’s Anion-Binding Site and the Mechanism of Outer Hair Cell Electromotility
Reviewer #1 (Public Review): Folding of Prestin’s Anion-Binding Site and the Mechanism of Outer Hair Cell Electromotility Open
Prestin responds to transmembrane voltage fluctuations by changing its cross-sectional area, a process underlying the electromotility of outer hair cells and cochlear amplification. Prestin belongs to the SLC26 family of anion transporters…