Now showing items 1-9 of 9
Aquaporins in Saccharomyces: Characterization of a second functional water channel protein
(National Academy of Sciences, 2001-01-30)
The Saccharomyces cerevisiae genome database contains two ORFs with homology to aquaporins, AQY1 and AQY2. Aqy1p has been shown to be a functional aquaporin in some strains, such as Sigma1278b. AQY2 is disrupted by a stop ...
Man is not a rodent: aquaporins in the airways
(American Thoracic Society, 2001-03)
Respiratory aquaporins in lung inflammation: the night is young
(American Thoracic Society, 2000-01)
Functional requirement of aquaporin-5 in plasma membranes of sweat glands
(National Academy of Sciences, 2002-01-08)
The distribution and function of aquaporins (AQPs) have not previously been defined in sweat glands. In this study, AQP1, AQP3, and AQP5 mRNA were demonstrated in rat paw by reverse transcription (RT)-PCR, but AQP2 and ...
Aquaporins and the respiratory system: advice for a lung investigator
(American Society for Clinical Investigation, 2000-01-01)
Aquaporin-4 square array assembly: Opposing actions of M1 and M23 isoforms
(National Academy of Sciences, 2003-11-11)
Osmotic homeostasis in the brain involves movement of water through aquaporin-4 (AQP4) membrane channels. Perivascular astrocyte end-feet contain distinctive orthogonal lattices (square arrays) assembled from 4- to 6-nm ...
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 ...
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 ...
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 ...