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PMID: 10698922 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, Non-P.H.S. Research Support, U.S. Gov't, P.H.S. Review

The importance of aquaporin water channel protein structures.

The EMBO journal ·Vol. 19 ·No. 5 ·2000-03-01 ·Pages 800-6

Engel A, Fujiyoshi Y, Agre P

Abstract

The history of the water channel and recent structural and functional analyses of aquaporins are reviewed. These ubiquitous channels are important for bacteria, plants and animals, exhibit a pronounced sequence homology and share functional as well as structural similarities. Aquaporins allow water or small specific solutes to pass unhindered, but block the passage of ions to prevent dissipation of the transmembrane potential. Besides advances in structure determination, recent experiments suggest that many of these channels are regulated by pH variations, phosphorylation and binding of auxiliary proteins.

MeSH Terms
Animals Aquaporins/chemistry,metabolism Humans Protein Conformation Structure-Activity Relationship
Chemicals
Aquaporins
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Engel A
M.E.Müller-Institute for Microscopy at the Biozentrum, University of Basel, CH-4056, Switzerland. [email protected]
Fujiyoshi Y
Agre P
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Article Info
Journal
The EMBO journal
Abbr.
EMBO J
ISSN
0261-4189
Published
2000-03-01
Pages
800-6
Language
English
Region
England
NLM ID
8208664
PMCID
PMC305620
Subset
IM
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