Browsing Nobel Prize Winners by Title
Now showing items 1-20 of 147
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Adenovirus-mediated Expression of Aquaporin-5 in Epithelial Cells
(American Society for Biochemistry and Molecular Biology, 1996-09-06)A recombinant adenovirus coding for rat aquaporin-5 was constructed and plaque purified. The recombinant adenovirus (AdrAQP5) mediated the expression of aquaporin-5 in rat and human salivary cell lines and in dog kidney ... -
An alpha-syntrophin-dependent pool of AQP4 in astroglial end-feet confers bidirectional water flow between blood and brain
(National Academy of Sciences, 2003-02-18)The water channel AQP4 is concentrated in perivascular and subpial membrane domains of brain astrocytes. These membranes form the interface between the neuropil and extracerebral liquid spaces. AQP4 is anchored at these ... -
Altered ubiquitination and stability of aquaporin-1 in hypertonic stress
(National Academy of Sciences, 2001-02-27)Aquaporin-1 (AQP1) water channel protein expression is increased by hypertonic stress. The contribution of changes in protein stability to hypertonic induction of AQP1 have not been described. Incubation of BALB/c fibroblasts ... -
Appearance of Water Channels in Xenopus Oocytes Expressing Red Cell CHIP28 Protein
(American Association for the Advancement of Science, 1992-04-17)Water rapidly crosses the plasma membrane of red blood cells (RBCs) and renal tubules through specialized channels. Although selective for water, the molecular structure of these channels is unknown. The CHIP28 protein is ... -
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 ... -
Aquaglyceroporin PbAQP during intraerythrocytic development of the malaria parasite Plasmodium berghei
(National Academy of Sciences, 2007-02-13)The malaria parasite can use host plasma glycerol for lipid biosynthesis and membrane biogenesis during the asexual intraerythrocytic development. The molecular basis for glycerol uptake into the parasite is undefined. We ... -
Aquaporin 9 is the major pathway for glycerol uptake by mouse erythrocytes, with implications for malarial virulence
(National Academy of Sciences, 2007-07-24)Human and rodent erythrocytes are known to be highly permeable to glycerol. Aquaglyceroporin aquaporin (AQP)3 is the major glycerol channel in human and rat erythrocytes. However, AQP3 expression has not been observed in ... -
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 ... -
Aquaporin null phenotypes: The importance of classical physiology
(National Academy of Sciences, 1998-08-04) -
Aquaporin water channels [Nobel Lecture]
(Gesellschaft Deutscher Chemiker, 2004) -
Aquaporin water channels: atomic structure molecular dynamics meet clinical medicine
(American Society for Clinical Investigation, 2002-06-01) -
Aquaporin Water Channels: Nobel Lecture, December 8, 2003
(© The Nobel Foundation 2003, 2003-12-08) -
Aquaporin-1 Water Channel Expression in Human Kidney
(American Society for Nephrology, 1997-01)The pattern of aquaporin-1 water channel protein (AQP1) expression in the human kidney was analyzed by immunocytochemistry using semi-thin and optimized high-resolution immunoelectron microscopy based on freeze-substituted ... -
Aquaporin-1 water channel protein in lung: ontogeny, steroid-induced expression, and distribution in rat
(American Society for Clinical Investigation, 1996-05-15)At birth water is rapidly reabsorbed from the distal lung in preparation for alveolar gas exchange. To investigate a potential role for the AQP1 water channel in development, lung membranes from fetal and perinatal rats ... -
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 ... -
Aquaporin-4 square array assembly: Opposing actions of M1 and M23 isoforms
(National Academy of Sciences, 2003-11-11)Osmotic homeostasis in the brain involves movement of water through aquaporin-4 (AQP4) membrane channels. Perivascular astrocyte end-feet contain distinctive orthogonal lattices (square arrays) assembled from 4- to 6-nm ... -
Aquaporin-4 water channel protein in the rat retina and optic nerve: polarized expression in Müller cells and fibrous astrocytes
(Society for Neuroscience, 1998-04-01)The water permeability of cell membranes differs by orders of magnitude, and most of this variability reflects the differential expression of aquaporin water channels. We have recently found that the CNS contains a member ... -
Aquaporin-6: An intracellular vesicle water channel protein in renal epithelia
(National Academy of Sciences, 1999-05-01)All characterized mammalian aquaporins (AQPs) are localized to plasma membranes where they function chiefly to mediate water transport across cells. Here we show that AQP6 is localized exclusively in intracellular membranes ... -
Aquaporins and the respiratory system: advice for a lung investigator
(American Society for Clinical Investigation, 2000-01-01) -
Aquaporins in complex tissues. I. Developmental patterns in respiratory and glandular tissues of rat
(American Physological Society, 1997-11)Developmental expression of aquaporin water transport proteins is not well understood in respiratory tract or secretory glands; here we define aquaporin protein ontogeny in rat. Expression of aquaporin-3 (AQP3), AQP4, and ...