Now showing items 1-7 of 7
Characterization of aquaporin-6 as a nitrate channel in mammilian cells: Requirement of pore-lining residue threonine 63
(American Society for Biochemistry and Molecular Biology, 2002-10-18)
Aquaporins (AQP) were originally regarded as plasma membrane channels that are freely permeated by water or small uncharged solutes but not by ions. Unlike other aquaporins, AQP6 overexpressed in Xenopus laevis oocytes was ...
Heterotetrameric composition of aquaporin-4 water channels.
(American Chemical Society, 1999-08-24)
Aquaporin (AQP) water channel proteins are tetrameric assemblies of individually active approximately 30 kDa subunits. AQP4 is the predominant water channel protein in brain, but immunoblotting of native tissues has ...
Aquaporin water channels [Nobel Lecture]
(Gesellschaft Deutscher Chemiker, 2004)
Conversion of aquaporin 6 from an anion channel to a water-selective channel by a single amino acid substitution
(National Academy of Sciences, 2005-02-08)
Aquaporin (AQP) 6 belongs to the aquaporin water channel family. Unlike other aquaporins, AQP6 functions not as a water channel but as an anion-selective channel. Single-channel analyses have shown AQP6 to flicker rapidly ...
Structural determinants of water permeation through aquaporin-1
(Nature Publishing Group, 2000-10-05)
Human red cell AQP1 is the first functionally defined member of the aquaporin family of membrane water channels. Here we describe an atomic model of AQP1 at 3.8A resolution from electron crystallographic data. Multiple ...
Structural basis for conductance by the archaeal aquaporin AqpM at 1.68 Å
(National Academy of Sciences, 2005-12-27)
To explore the structural basis of the unique selectivity spectrum and conductance of the transmembrane channel protein AqpM from the archaeon Methanothermobacter marburgensis, we determined the structure of AqpM to 1.68-A ...
Aquaporin water channels: atomic structure molecular dynamics meet clinical medicine
(American Society for Clinical Investigation, 2002-06-01)