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    The human Aquaporin-5 gene. Molecular characterization and chromosomal localization. 

    Yonescu, Raluca; Lee, M. Douglas; Jenkins, Nancy A.; Raina, Surabhi; Griffin, Constance A.; Copeland, Neal G.; Gilbert, Debra J.; Bhakta, Kushal Y.; Agre, Peter; Preston, Gregory M. (American Society for Biochemistry and Molecular Biology, 1996-04-12)
    The cDNA for the fifth mammalian aquaporin (AQP5) was isolated from rat, and expression was demonstrated in rat salivary and lacrimal glands, cornea, and lung (Raina, S., Preston, G. M., Guggino, W. B., and Agre, P. (1995) ...
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    Quantification of Aquaporin-CHIP water channel protein in microdissected renal tubules by fluorescence-based ELISA 

    Knepper, Mark A.; Agre, Peter; Smith, Barbara L.; Maeda, Yoshitaka (American Society for Clinical Investigation, 1995-01)
    Several transporters have been localized along the nephron by physiological methods or immunocytochemistry. However, the actual abundance of these molecules has not been established. To accomplish this goal, we have developed ...
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    Reconstitution of functional water channels in liposomes containing purified red cell CHIP28 protein 

    Agre, Peter; Smith, Barbara L.; Ambudkar, Suresh V.; Zeidel, Mark L. (American Chemical Society, 1992)
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    Aquaporin-4 water channel protein in the rat retina and optic nerve: polarized expression in Müller cells and fibrous astrocytes 

    Ottersen, O. P.; Agre, P; Nielsen, S; Laake, J. H.; Haug, F. M.; Torp, R.; Veruki, M. L.; Nagelhus, E. A. (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 ...
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    The three-dimensional structure of aquaporin-1 

    Engel, Andreas; Agre, Peter; Smith, Barbara L.; Fujiyoshi, Yoshinori; Mitsuoka, Kaoru; Heymann, J. Bernard; Murata, Kazuyoshi; Hirai, Teruhisa; Walz, Thomas (Nature Publishing Group, 1997-06-05)
    The entry and exit of water from cells is a fundamental process of life. Recognition of the high water permeability of red blood cells led to the proposal that specialized water pores exist in the plasma membrane. Expression ...
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    Aquaporins in complex tissues. I. Developmental patterns in respiratory and glandular tissues of rat 

    Agre, Peter; Nielsen, Søren; King, Landon S. (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 ...
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    Water channel properties of major intrinsic protein of lens 

    Guggino, W B; Mulders, S. M.; Preston, G M; Deen, P. M.; Agre, P; Van Os, C. H. (American Society for Biochemistry and Molecular Biology, 1995-04-14)
    The functions of major intrinsic protein (MIP) of lens are still unresolved; however the sequence homology with channel-forming integral membrane protein (CHIP) and other Aquaporins suggests that MIP is a water channel. ...
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    Molecular Cloning and Characterization of an Aquaporin cDNA from Salivary, Lacrimal, and Respiratory Tissues 

    Preston, Gregory M.; Raina, Surabhi; Agre, Peter; Guggino, William B. (American Society for Biochemistry and Molecular Biology, 1995-01-27)
    The Aquaporin family of water channels plays a fundamental role in transmembrane water movements in numerous plant and animal tissues. Since the molecular pathway by which water is secreted by salivary glands is unknown, ...
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    Human red cell aquaporin CHIP. I. Molecular characterization of ABH and Colton blood group antigens 

    Agre, Peter; Anstee, David J.; Spring, Frances A.; Preston, Gregory M.; Smith, Barbara L. (American Society for Clinical Investigation, 1994-09)
    Blood group antigens are structural variants in surface carbohydrate or amino acid polymorphisms on extracellular domains of membrane proteins. The red cell water channel-forming integral protein (Aquaporin CHIP) is a ...
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    Cholangiocytes express the aquaporin CHIP and transport water via a channel-mediated mechanism 

    LaRusso, Nicholas F.; Agre, Peter; Alpini, Gianfranco; Pham, Linh; Ueno, Yoshiyuki; Yano, Motoyoshi; Roberts, Stuart K. (National Academy of Sciences, 1994-12-20)
    Cholangiocytes line the intrahepatic bile ducts and regulate salt and water secretion during bile formation, but the mechanism(s) regulating ductal water movement remains obscure. A water-selective channel, the aquaporin ...
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    AuthorAgre, Peter (40)Preston, Gregory M. (15)Smith, Barbara L. (15)Guggino, William B. (8)Nielsen, Søren (7)Jung, Jin Sup (4)King, Landon S. (4)Zeidel, Mark L. (4)Lee, M. Douglas (3)Agre, P (2)... View MoreSubject
    Aquaporins (43)
    Ion Channels/genetics (9)Water/metabolism (7)Ion Channels/biosynthesis (6)Membrane Proteins (6)Erythrocyte Membrane/metabolism (4)Ion Channels/metabolism (4)Escherichia coli Proteins (3)Ion Channels/analysis (3)Ion Channels/chemistry (3)... View MoreDate Issued2000 - 2003 (2)1991 - 1999 (41)Has File(s)Yes (43)

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