New roles for old holes: Ion channel function in aquaporin-1

dc.contributor.author	Yool, A.
dc.contributor.author	Weinstein, A.
dc.date.issued	2002
dc.description	© 2002 Int. Union Physiol. Sci./Am. Physiol. Soc.
dc.description.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.
dc.description.statementofresponsibility	Andrea J. Yool and Alan M. Weinstein
dc.identifier.citation	Physiology, 2002; 17(2):68-72
dc.identifier.doi	10.1152/nips.01372.2001
dc.identifier.issn	1548-9213
dc.identifier.issn	1522-161X
dc.identifier.orcid	Yool, A. [0000-0003-1283-585X]
dc.identifier.uri	http://hdl.handle.net/2440/47274
dc.language.iso	en
dc.publisher	American Physiological Society
dc.source.uri	https://doi.org/10.1152/nips.01372.2001
dc.subject	Animals
dc.subject	Humans
dc.subject	Water
dc.subject	Aquaporins
dc.subject	Blood Group Antigens
dc.subject	Amino Acid Sequence
dc.subject	Protein Conformation
dc.subject	Molecular Sequence Data
dc.subject	Aquaporin 1
dc.title	New roles for old holes: Ion channel function in aquaporin-1
dc.type	Journal article
pubs.publication-status	Published

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