Now showing items 1-10 of 45
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 ...
Reduced arsenic clearance and increased toxicity in aquaglyceroporin-9-null mice
(National Academy of Sciences, 2009-09-15)
Expressed in liver, aquaglyceroporin-9 (AQP9) is permeated by glycerol, arsenite, and other small, neutral solutes. To evaluate a possible protective role, AQP9-null mice were evaluated for in vivo arsenic toxicity. After ...
(© The Nobel Foundation 2003, 2003)
Delayed onset of brain edema and mislocalization of aquaporin-4 in dystrophin-null transgenic mice
(National Academy of Sciences, 2002-10-01)
Cerebral water accumulation was studied during induction of brain edema in dystrophin-null transgenic mice (mdx-betageo) and control mice. Immunofluorescence and immunoelectron microscopic analyses of dystrophin-null brains ...
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 ...
Aquaporin-11: a channel protein lacking apparent transport function expressed in brain
(BioMed Central, 2006-05)
BACKGROUND: The aquaporins are a family of integral membrane proteins composed of two subfamilies: the orthodox aquaporins, which transport only water, and the aquaglyceroporins, which transport glycerol, urea, or other ...
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 ...
How to Win the Nobel Prize?
(Public Library of Science, 2006-10)
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 ...