Please use this identifier to cite or link to this item: https://hdl.handle.net/2440/47274
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Type: Journal article
Title: New roles for old holes: Ion channel function in aquaporin-1
Author: Yool, A.
Weinstein, A.
Citation: Physiology, 2002; 17(2):68-72
Publisher: American Physiological Society
Issue Date: 2002
ISSN: 1548-9213
1522-161X
Statement of
Responsibility: 
Andrea J. Yool and Alan M. Weinstein
Abstract: Mammalian aquaporins are part of the diverse major intrinsic protein family of water and solute channels. Intriguing links exist in structural and functional properties between aquaporins and ion channels. A novel role for aquaporin-1 as a gated ion channel reshapes our current views of this ancient family of transmembrane channel proteins.
Keywords: Animals
Humans
Water
Aquaporins
Blood Group Antigens
Amino Acid Sequence
Protein Conformation
Molecular Sequence Data
Aquaporin 1
Description: © 2002 Int. Union Physiol. Sci./Am. Physiol. Soc.
DOI: 10.1152/nips.01372.2001
Published version: http://dx.doi.org/10.1152/nips.01372.2001
Appears in Collections:Aurora harvest
Molecular and Biomedical Science publications

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