Now showing items 1-7 of 7
Aquaporin water channels: atomic structure molecular dynamics meet clinical medicine
(American Society for Clinical Investigation, 2002-06-01)
Water and ion permeation of aquaporin-1 in planar lipid bilayers. Major differences in structural determinants and stoichiometry.
(American Society for Biochemistry and Molecular Biology, 2001-08-24)
The aquaporin-1 (AQP1) water channel protein is known to facilitate the rapid movement of water across cell membranes, but a proposed secondary role as an ion channel is still unsettled. Here we describe a method to ...
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 ...
Functional expression and characterization of an archaeal aquaporin. AqpM from methanothermobacter marburgensis.
(American Society for Biochemistry and Molecular Biology, 2003-03-21)
Researchers have described aquaporin water channels from diverse eubacterial and eukaryotic species but not from the third division of life, Archaea. Methanothermobacter marburgensis is a methanogenic archaeon that thrives ...
Aquaglyceroporin AQP9: solute permeation and metabolic control of expression in liver
(National Academy of Sciences, 2003-03-04)
Aquaglyceroporins form the subset of the aquaporin water channel family that is permeable to glycerol and certain small, uncharged solutes. AQP9 has unusually broad solute permeability and is expressed in hepatocyte plasma ...
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 ...
Ion Permeation of AQP6 Water Channel Protein: Single-Channel Recordings After Hg2+ Activation
(American Society for Biochemistry and Molecular Biology, 2002-08-09)
Aquaporin-6 (AQP6) has recently been identified as an intracellular vesicle water channel with anion permeability that is activated by low pH or HgCl2. Here we present direct evidence of AQP6 channel gating using patch ...