Now showing items 1-8 of 8
Functional impairment of lens aquaporin in two families with dominantly inherited cataracts
(Oxford University Press, 2000-09-22)
Opacities in the crystalline lens of eye appear with high frequency in the general population. Dominantly inherited cataracts with differing clinical features were found in two families carrying different point mutations ...
Aquaporin-6: An intracellular vesicle water channel protein in renal epithelia
(National Academy of Sciences, 1999-05-01)
All characterized mammalian aquaporins (AQPs) are localized to plasma membranes where they function chiefly to mediate water transport across cells. Here we show that AQP6 is localized exclusively in intracellular membranes ...
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 ...
Aquaporin water channels: atomic structure molecular dynamics meet clinical medicine
(American Society for Clinical Investigation, 2002-06-01)
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 ...
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 ...
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 ...
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 ...