Results 261 to 270 of about 38,099 (293)
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Aquaporin 6 is permeable to glycerol and urea

Pfl�gers Archiv European Journal of Physiology, 2004
The passive water permeability ( L(p)) of AQP6 is activated by Hg(2+). Our aim was to test if L(p) was associated with a permeability to small hydrophilic molecules such as glycerol and urea. AQP6 was expressed in Xenopus laevis oocytes and activated by 0.3 mM of HgCl(2) in the bathing solution.
Holm, L. M.   +2 more
openaire   +2 more sources

Presence and localization of aquaporin-6 in rat parotid acinar cells

Cell and Tissue Research, 2008
Aquaporins (AQPs) are integral membrane proteins that function as channels for the transfer of water and small solutes across membranes. In mammalian cells, 13 isoforms (AQP0-12) have been identified, and these exhibit unique patterns of expression in various cell types and tissues.
Miwako, Matsuki-Fukushima   +5 more
openaire   +2 more sources

Water channel activity of putative aquaporin‐6 present in Aedes aegypti

Archives of Insect Biochemistry and Physiology, 2018
AbstractAquaporins (AQPs) are integral membrane channels that facilitate the bidirectional transport of water and sometimes other small solutes across biological membranes. AQPs are important in mediating environmental adaptations in mosquitoes and are considered as a novel target for the development of effective insecticides against mosquitoes.
Sandhya Sreedharan   +1 more
openaire   +2 more sources

Aquaporin-1 Deletion in Mice Inhibits Hepa1-6 Hepatocellular Carcinoma Growth

2009 3rd International Conference on Bioinformatics and Biomedical Engineering, 2009
Aquaporin (AQP) has been reported to express in microvessels of many different type of tumor, indicating the possible involvement of AQP in tumor angiogenesis. Tumor angiogenesis is a mandatory step of tumor growth involving endothelial cell proliferation and migration from blood vessels in peritumoral tissues and formation of tubules. A murine Hepal-6
Yong Jiang   +4 more
openaire   +1 more source

pH Regulated Anion Permeability of Aquaporin-6

2008
The kidney is a model organ for transport physiology (Nielsen 1996). AQPs are well-characterized in mammalian kidneys, where they facilitate transepithelial water reabsorption. Most renal AQPs are expressed either in proximal tubule cells or in collecting duct principal cells, which are known as sites for water reabsorption.
openaire   +2 more sources

6-Hydroxydopamine leads to T2 hyperintensity, decreased claudin-3 immunoreactivity and altered aquaporin 4 expression in the striatum

Behavioural Brain Research, 2012
The neurotoxin 6-hydroxydopamine (6-OHDA) is frequently used in animal models to mimic Parkinson's disease. Imaging studies describe hyperintense signalling in regions close to the site of the 6-OHDA injection in T2-weighted (T2w) magnetic resonance imaging (MRI). The nature of this hyperintense signal remains elusive and still is matter of discussion.
Wachter, Britta   +11 more
openaire   +3 more sources

Kallikrein 6 and Aquaporin 1 in Normal Human Nephrogenesis and Congenital Anomalies of the Kidneys and Urinary Tract

Pediatric Nephrology
Aims/Purpose: Kallikrein 6 (KLK6) is a protease involved in multiple biological processes. It is highly expressed in the brain, kidneys, and pancreas. Aquaporin 1 (AQP1) is a water channel protein expressed in the proximal tubules for water reabsorption.
Vukojević, Katarina   +8 more
openaire   +1 more source

Effects of feed and draw solution temperature on the performance of Aquaporin HFFO.6 membrane in forward osmosis

Materials Today: Proceedings, 2023
Dsilva Winfred Rufuss, D.   +2 more
openaire   +1 more source

Targeting Aquaporin-4 Subcellular Localization to Treat Central Nervous System Edema

Cell, 2020
Philip Kitchen   +2 more
exaly  

Phosphorylation of a wheat aquaporin at two sites enhances both plant growth and defense

Molecular Plant, 2022
Baoyan Li, Weiyang Wang, Hansong Dong
exaly  

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