Now showing items 1-10 of 19
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 ...
The Rh polypeptide is a major fatty acid-acylated erythrocyte membrane protein
(American Society for Biochemistry and Molecular Biology, 1988-12-05)
The erythrocyte Rh antigens contain an Mr = 32,000 integral protein which is thought to contribute in some way to the organization of surrounding phospholipid. To search for possible fatty acid acylation of the Rh polypeptide, ...
Appearance of Water Channels in Xenopus Oocytes Expressing Red Cell CHIP28 Protein
(American Association for the Advancement of Science, 1992-04-17)
Water rapidly crosses the plasma membrane of red blood cells (RBCs) and renal tubules through specialized channels. Although selective for water, the molecular structure of these channels is unknown. The CHIP28 protein is ...
Mutations in aquaporin-1 in phenotypically normal humans without functional CHIP water channels
(American Association for the Advancement of Science, 1994-09-09)
The gene aquaporin-1 encodes channel-forming integral protein (CHIP), a member of a large family of water transporters found throughout nature. Three rare individuals were identified who do not express CHIP-associated ...
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 ...
Deficient red-cell spectrin in severe, recessively inherited spherocytosis
(Massachusetts Medical Society, 1982-05-13)
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 ...
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)