Now showing items 1-10 of 59
Aquaporin water channels: atomic structure molecular dynamics meet clinical medicine
(American Society for Clinical Investigation, 2002-06-01)
Targeted disruption of the Cl−/HCO3− exchanger Ae2 results in osteopetrosis in mice
(National Academy of Sciences, 2009-02-03)
Osteoclasts are multinucleated bone-resorbing cells responsible for constant remodeling of bone tissue and for maintaining calcium homeostasis. The osteoclast creates an enclosed space, a lacuna, between their ruffled ...
Highly selective water channel activity measured by voltage clamp: Analysis of planar lipid bilayers reconstituted with purified AqpZ
(National Academy of Sciences, 2001-08-14)
Aquaporins are membrane channels selectively permeated by water or water plus glycerol. Conflicting reports have described ion conductance associated with some water channels, raising the question of whether ion conductance ...
Hypertonic induction of aquaporin-5 expression through an ERK-dependent pathway
(American Society for Biochemistry and Molecular Biology, 2000-03-24)
Aquaporin-5 (AQP5) is a water channel protein expressed in lung, salivary gland, and lacrimal gland epithelia. Each of these sites may experience fluctuations in surface liquid osmolarity; however, osmotic regulation of ...
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 ...
Structural basis for conductance by the archaeal aquaporin AqpM at 1.68 Å
(National Academy of Sciences, 2005-12-27)
To explore the structural basis of the unique selectivity spectrum and conductance of the transmembrane channel protein AqpM from the archaeon Methanothermobacter marburgensis, we determined the structure of AqpM to 1.68-A ...
Aquaporin expression and freeze tolerance in Candida albicans
(American Society for Microbiology, 2005-10)
Aquaporins are members of the major intrinsic protein superfamily of integral membrane proteins which enable the transport of water, glycerol, and other solutes across membranes in various organisms. In microorganisms, the ...
Man is not a rodent: aquaporins in the airways
(American Thoracic Society, 2001-03)
Aquaporin water channels [Nobel Lecture]
(Gesellschaft Deutscher Chemiker, 2004)
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 ...