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Diflunisal inhibits prestin by chloride-dependent mechanism

Diflunisal inhibits prestin by chloride-dependent mechanism

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_plos_journals_1930442043

Diflunisal inhibits prestin by chloride-dependent mechanism

About this item

Full title

Diflunisal inhibits prestin by chloride-dependent mechanism

Publisher

United States: Public Library of Science

Journal title

PloS one, 2017-08, Vol.12 (8), p.e0183046-e0183046

Language

English

Formats

Publication information

Publisher

United States: Public Library of Science

More information

Scope and Contents

Contents

The motor protein prestin is a member of the SLC26 family of anion antiporters and is essential to the electromotility of cochlear outer hair cells and for hearing. The only direct inhibitor of electromotility and the associated charge transfer is salicylate, possibly through direct interaction with an anion-binding site on prestin. In a screen to...

Alternative Titles

Full title

Diflunisal inhibits prestin by chloride-dependent mechanism

Authors, Artists and Contributors

Identifiers

Primary Identifiers

Record Identifier

TN_cdi_plos_journals_1930442043

Permalink

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_plos_journals_1930442043

Other Identifiers

ISSN

1932-6203

E-ISSN

1932-6203

DOI

10.1371/journal.pone.0183046

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