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Cryo-EM structures and functional characterization of murine Slc26a9 reveal mechanism of uncoupled c...

Cryo-EM structures and functional characterization of murine Slc26a9 reveal mechanism of uncoupled c...

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_doaj_primary_oai_doaj_org_article_dbe2fb604f9d45c8a7fe11a823aff74f

Cryo-EM structures and functional characterization of murine Slc26a9 reveal mechanism of uncoupled chloride transport

About this item

Full title

Cryo-EM structures and functional characterization of murine Slc26a9 reveal mechanism of uncoupled chloride transport

Publisher

England: eLife Science Publications, Ltd

Journal title

eLife, 2019-07, Vol.8

Language

English

Formats

Publication information

Publisher

England: eLife Science Publications, Ltd

More information

Scope and Contents

Contents

The epithelial anion transporter SLC26A9 contributes to airway surface hydration and gastric acid production. Colocalizing with CFTR, SLC26A9 has been proposed as a target for the treatment of cystic fibrosis. To provide molecular details of its transport mechanism, we present cryo-EM structures and a functional characterization of murine Slc26a9....

Alternative Titles

Full title

Cryo-EM structures and functional characterization of murine Slc26a9 reveal mechanism of uncoupled chloride transport

Authors, Artists and Contributors

Identifiers

Primary Identifiers

Record Identifier

TN_cdi_doaj_primary_oai_doaj_org_article_dbe2fb604f9d45c8a7fe11a823aff74f

Permalink

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_doaj_primary_oai_doaj_org_article_dbe2fb604f9d45c8a7fe11a823aff74f

Other Identifiers

ISSN

2050-084X

E-ISSN

2050-084X

DOI

10.7554/eLife.46986

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