Now showing items 1-3 of 3
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 ...
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 ...
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 ...