Artikel ; Online: Folding of prestin's anion-binding site and the mechanism of outer hair cell electromotility.
2023 Band 12
Abstract: 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 yet is the ... ...
| Abstract | 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 yet is the only member capable of displaying electromotility. Prestin's voltage-dependent conformational changes are driven by the putative displacement of residue R399 and a set of sparse charged residues within the transmembrane domain, following the binding of a Cl |
|---|---|
| Mesh-Begriff(e) | Hair Cells, Auditory, Outer ; Anions ; Binding Sites ; Cochlea ; Lipid Bilayers ; Membrane Transport Proteins |
| Chemische Substanzen | Anions ; Lipid Bilayers ; Membrane Transport Proteins |
| Sprache | Englisch |
| Erscheinungsdatum | 2023-12-06 |
| Erscheinungsland | England |
| Dokumenttyp | Journal Article |
| ZDB-ID | 2687154-3 |
| ISSN | 2050-084X ; 2050-084X |
| ISSN (online) | 2050-084X |
| ISSN | 2050-084X |
| DOI | 10.7554/eLife.89635 |
| Datenquelle | MEDical Literature Analysis and Retrieval System OnLINE |
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