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Aquaporin water channels--from atomic structure to clinical medicine

Agre, P. and King, L. S. and Yasui, M. and Guggino, W. B. and Ottersen, O. P. and Fujiyoshi, Y. and Engel, A. and Nielsen, S.. (2002) Aquaporin water channels--from atomic structure to clinical medicine. The journal of physiology, Vol. 542, H. 1. pp. 3-16.

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Official URL: http://edoc.unibas.ch/dok/A5262387

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Abstract

The water permeability of biological membranes has been a longstanding problem in physiology, but the proteins responsible for this remained unknown until discovery of the aquaporin 1 (AQP1) water channel protein. AQP1 is selectively permeated by water driven by osmotic gradients. The atomic structure of human AQP1 has recently been defined. Each subunit of the tetramer contains an individual aqueous pore that permits single-file passage of water molecules but interrupts the hydrogen bonding needed for passage of protons. At least 10 mammalian aquaporins have been identified, and these are selectively permeated by water (aquaporins) or water plus glycerol (aquaglyceroporins). The sites of expression coincide closely with the clinical phenotypes--ranging from congenital cataracts to nephrogenic diabetes insipidus. More than 200 members of the aquaporin family have been found in plants, microbials, invertebrates and vertebrates, and their importance to the physiology of these organisms is being uncovered.
Faculties and Departments:05 Faculty of Science > Departement Biozentrum > Former Organization Units Biozentrum > Structural Biology (Engel)
UniBasel Contributors:Engel, Andreas H
Item Type:Article, refereed
Article Subtype:Research Article
Bibsysno:Link to catalogue
Publisher:Blackwell
ISSN:1469-7793
Note:Publication type according to Uni Basel Research Database: Journal article
Last Modified:11 Oct 2012 15:15
Deposited On:22 Mar 2012 13:23

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