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, 2004The 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
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Presence and localization of aquaporin-6 in rat parotid acinar cells
Cell and Tissue Research, 2008Aquaporins (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
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Water channel activity of putative aquaporin‐6 present in Aedes aegypti
Archives of Insect Biochemistry and Physiology, 2018AbstractAquaporins (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
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Aquaporin-1 Deletion in Mice Inhibits Hepa1-6 Hepatocellular Carcinoma Growth
2009 3rd International Conference on Bioinformatics and Biomedical Engineering, 2009Aquaporin (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
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pH Regulated Anion Permeability of Aquaporin-6
2008The 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.
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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
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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
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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
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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
Targeting Aquaporin-4 Subcellular Localization to Treat Central Nervous System Edema
Cell, 2020Philip Kitchen +2 more
exaly
Phosphorylation of a wheat aquaporin at two sites enhances both plant growth and defense
Molecular Plant, 2022Baoyan Li, Weiyang Wang, Hansong Dong
exaly

