Now showing items 1-10 of 11
The mercury-sensitive residue at cysteine 189 in the CHIP28 water channel
(American Society for Biochemistry and Molecular Biology, 1993-01-05)
Water channels provide the plasma membranes of red cells and renal proximal tubules with high permeability to water, thereby permitting water to move in the direction of an osmotic gradient. Molecular identification of ...
Aquaporins in Saccharomyces: Genetic and functional distinctions between laboratory and wild-type strains
(American Society for Biochemistry and Molecular Biology, 1998-10-16)
Aquaporin water channel proteins mediate the transport of water across cell membranes in numerous species. The Saccharomyces genome data base contains an open reading frame (here designated AQY1) that encodes a protein ...
Reconstitution of functional water channels in liposomes containing purified red cell CHIP28 protein
(American Chemical Society, 1992)
Molecular cloning and characterization of AqpZ, a water channel from Escherichia coli
(American Society for Biochemistry and Molecular Biology, 1995-12-08)
The aquaporin family of molecular water channels is widely expressed throughout the plant and animal kingdoms. No bacterial aquaporins are known; however, sequence-related bacterial genes have been identified that encode ...
Highly selective water channel activity measured by voltage clamp: Analysis of planar lipid bilayers reconstituted with purified AqpZ
(National Academy of Sciences, 2001-08-14)
Aquaporins are membrane channels selectively permeated by water or water plus glycerol. Conflicting reports have described ion conductance associated with some water channels, raising the question of whether ion conductance ...
Cholangiocytes express the aquaporin CHIP and transport water via a channel-mediated mechanism
(National Academy of Sciences, 1994-12-20)
Cholangiocytes line the intrahepatic bile ducts and regulate salt and water secretion during bile formation, but the mechanism(s) regulating ductal water movement remains obscure. A water-selective channel, the aquaporin ...
Reconstitution and functional comparison of purified GlpF and AqpZ, the glycerol and water channels from Escherichia coli
(National Academy of Sciences, 2001-02-27)
A large family of membrane channel proteins selective for transport of water (aquaporins) or water plus glycerol (aquaglyceroporins) has been found in diverse life forms. Escherichia coli has two members of this family-a ...
Specialized membrane domains for water transport in glial cells: high resolution immunogold cytochemistry of aquaporin-4 in rat brain
(Copyright held by the original publisher: Journal of Neuroscience, 1997-01-01)
Membrane water transport is critically involved in brain volume homeostasis and in the pathogenesis of brain edema. The cDNA encoding aquaporin-4 (AQP4) water channel protein was recently isolated from rat brain. We used ...
Molecular dissection of water and glycerol permeability of the aquaglyceroporin from Plasmodium falciparum by mutational analysis
(National Academy of Sciences, 2004-02-03)
The selectivity of aquaporins for water and solutes is determined by pore diameter. Paradoxically, the wider pores of glycerol facilitators restrict water passage by an unknown mechanism. Earlier we characterized an ...
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 ...