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Cited by 1,256

The DOI matches its Crossref record; 530 of the 530 references it cites were found in a registry or an index.

Molecular Structure and Physiological Function of Chloride Channels

Jentsch, Thomas J., Stein, Valentin, Weinreich, Frank, Zdebik, Anselm A.·2002·Physiological Reviews

Abstract

Cl−channels reside both in the plasma membrane and in intracellular organelles. Their functions range from ion homeostasis to cell volume regulation, transepithelial transport, and regulation of electrical excitability. Their physiological roles are impressively illustrated by various inherited diseases and knock-out mouse models. Thus the loss of distinct Cl−channels leads to an impairment of transepithelial transport in cystic fibrosis and Bartter's syndrome, to increased muscle excitability in myotonia congenita, to reduced endosomal acidification and impaired endocytosis in Dent's disease, and to impaired extracellular acidification by osteoclasts and osteopetrosis. The disruption of several Cl−channels in mice results in blindness. Several classes of Cl−channels have not yet been identified at the molecular level. Three molecularly distinct Cl−channel families (CLC, CFTR, and ligand-gated GABA and glycine receptors) are well established. Mutagenesis and functional studies have yielded considerable insights into their structure and function. Recently, the detailed structure of bacterial CLC proteins was determined by X-ray analysis of three-dimensional crystals. Nonetheless, they are less well understood than cation channels and show remarkably different biophysical and structural properties. Other gene families (CLIC or CLCA) were also reported to encode Cl−channels but are less well characterized. This review focuses on molecularly identified Cl−channels and their physiological roles.

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Crossref · 10.1152/physrev.00029.2001

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Metadata

Authors
Jentsch, T. J., Stein, V., Weinreich, F., & Zdebik, A. A.
Venue
Physiological Reviews
Published
2002-04-01
Volume
82
Issue
2
Pages
503-568
ISSN
  • 0031-9333 (ISSN-L)
  • 1522-1210
OpenAlex
W2135426025
Cited by
1,256
References
530
FWCI
5.74
Type
journal article
Language
en
Open access
closed

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