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    Highly selective water channel activity measured by voltage clamp: Analysis of planar lipid bilayers reconstituted with purified AqpZ 

    Agre, P; Borgnia, M. J.; Saparov, S. M.; Pohl, P (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 ...
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    Heterotetrameric composition of aquaporin-4 water channels. 

    Agre, Peter; Nielsen, S; Christensen, B. M.; Neely, JD (American Chemical Society, 1999-08-24)
    Aquaporin (AQP) water channel proteins are tetrameric assemblies of individually active approximately 30 kDa subunits. AQP4 is the predominant water channel protein in brain, but immunoblotting of native tissues has ...
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    Rapid gating and anion permeability of an intracellular aquaporin 

    Agre, Peter; Guggino, WB; Nielsen, S; Kwon, TH; Hazama, A.; Yasui, M. (Nature Publishing Group, 1992-11-11)
    Aquaporin (AQP) water-channel proteins are freely permeated by water but not by ions or charged solutes. Although mammalian aquaporins were believed to be located in plasma membranes, rat AQP6 is restricted to intracellular ...
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    Aquaporin expression and freeze tolerance in Candida albicans 

    Van Dijck, P.; Thevelein, J. M.; Agre, P; Carbrey, J. M.; Tanghe, A. (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 ...
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    Conversion of aquaporin 6 from an anion channel to a water-selective channel by a single amino acid substitution 

    Yasui, Masato; Hazama, Akihiro; Agre, Peter; Kato, Yasuhiro; Kozono, David; Liu, Kun (National Academy of Sciences, 2005-02-08)
    Aquaporin (AQP) 6 belongs to the aquaporin water channel family. Unlike other aquaporins, AQP6 functions not as a water channel but as an anion-selective channel. Single-channel analyses have shown AQP6 to flicker rapidly ...
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    Functional requirement of aquaporin-5 in plasma membranes of sweat glands 

    Nielsen, Søren; Agre, Peter C.; King, Landon S.; Menon, Anil G.; Krane, Carissa M.; Frøkiær, Jørgen; Fumagalli, Ornella; Jensen, Uffe B.; Kwon, Tae-Hwan; Nejsum, Lene N. (National Academy of Sciences, 2002-01-08)
    The distribution and function of aquaporins (AQPs) have not previously been defined in sweat glands. In this study, AQP1, AQP3, and AQP5 mRNA were demonstrated in rat paw by reverse transcription (RT)-PCR, but AQP2 and ...
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    Altered ubiquitination and stability of aquaporin-1 in hypertonic stress 

    King, Landon S.; Agre, Peter; Leitch, Virginia (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 ...
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    Aquaporin-6: An intracellular vesicle water channel protein in renal epithelia 

    Kwon, Tae-Hwan; Nielsen, Søren; Agre, Peter; Knepper, Mark A.; Yasui, Masato (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 ...
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    Aquaporin 9 is the major pathway for glycerol uptake by mouse erythrocytes, with implications for malarial virulence 

    Carbrey, Jennifer M.; Agre, Peter; King, Landon S.; Nielsen, Søren; Frøkiær, Jørgen; Kumar, Nirbhay; Rojek, Aleksandra; Promeneur, Dominique; Liu, Yangjian (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 ...
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    Defective glycerol metabolism in aquaporin 9 (AQP9) knockout mice 

    Nielsen, S; Frøkiær, Jørgen; Agre, Peter; Fenton, R. A.; Füchtbauer, A C; Furman, C. Sue; Skowronski, M. T.; Rojek, A M (National Academy of Sciences, 2007-02-27)
    Aquaporin-9 (AQP9) is an aquaglyceroporin membrane channel shown biophysically to conduct water, glycerol, and other small solutes. Because the physiological role/s of AQP9 remain undefined and the expression sites of AQP9 ...
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    AuthorAgre, Peter (13)King, Landon S. (4)Kozono, David (4)Carbrey, Jennifer M. (3)Frøkiær, Jørgen (3)Nielsen, S (3)Nielsen, Søren (3)Yasui, Masato (3)Agre, P (2)Hazama, Akihiro (2)... View MoreSubject
    Aquaporins/metabolism (16)
    Membrane Proteins (3)Aquaporins/chemistry (2)Aquaporins/physiology (2)Glycerol/metabolism (2)Liver/metabolism (2)Water/metabolism (2)Amino Acid Substitution (1)Aquaporins/genetics (1)Arsenites/metabolism (1)... View MoreDate Issued2000 - 2007 (13)1992 - 1999 (3)Has File(s)Yes (16)

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