Now showing items 21-30 of 100
The three-dimensional structure of aquaporin-1
(Nature Publishing Group, 1997-06-05)
The entry and exit of water from cells is a fundamental process of life. Recognition of the high water permeability of red blood cells led to the proposal that specialized water pores exist in the plasma membrane. Expression ...
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 ...
Aquaporins in complex tissues. I. Developmental patterns in respiratory and glandular tissues of rat
(American Physological Society, 1997-11)
Developmental expression of aquaporin water transport proteins is not well understood in respiratory tract or secretory glands; here we define aquaporin protein ontogeny in rat. Expression of aquaporin-3 (AQP3), AQP4, and ...
Rapid gating and anion permeability of an intracellular aquaporin
(Nature Publishing Group, 1992-11-11)
Aquaporin (AQP) water-channel proteins are freely permeated by water but not by ions or charged solutes. Although mammalian aquaporins were believed to be located in plasma membranes, rat AQP6 is restricted to intracellular ...
Linkage of dominant hereditary spherocytosis to the gene for the erythrocyte membrane-skeleton protein ankyrin
(Massachusetts Medical Society, 1990-10-11)
Reconstitution of functional water channels in liposomes containing purified red cell CHIP28 protein
(American Chemical Society, 1992)
Aquaporin water channels [Nobel Lecture]
(Gesellschaft Deutscher Chemiker, 2004)
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 ...
Bepridil and cetiedil. Vasodilators which inhibit Ca2+-dependent calmodulin interactions with erythrocyte membranes
(American Society for Clinical Investigation, 1984-09)
Two new vascular smooth muscle relaxants, bepridil and cetiedil, were found to possess specific CaM-inhibitory properties which resembled those of trifluoperazine. Trifluoperazine, bepridil, and cetiedil inhibited ...
Isolation of the cDNA for erythrocyte integral membrane protein of 28 kilodaltons: member of an ancient channel family
(National Academy of Sciences, 1991-12-15)
CHIP28 is a 28-kDa integral membrane protein with similarities to membrane channels and is found in erythrocytes and renal tubules. A cDNA for CHIP28 was isolated from human fetal liver cDNA template by a three-step ...