Now showing items 1-10 of 10

    • Appearance of Water Channels in Xenopus Oocytes Expressing Red Cell CHIP28 Protein 

      Agre, Peter; Guggino, William B.; Carroll, Tiziana Piazza; Preston, Gregory M. (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 ...
    • Characterization of aquaporin-6 as a nitrate channel in mammilian cells: Requirement of pore-lining residue threonine 63 

      Yasui, Masato; Agre, Peter; Guggino, William B.; Kozono, David; Beitz, Eric; Ikeda, Masahiro (American Society for Biochemistry and Molecular Biology, 2002-10-18)
      Aquaporins (AQP) were originally regarded as plasma membrane channels that are freely permeated by water or small uncharged solutes but not by ions. Unlike other aquaporins, AQP6 overexpressed in Xenopus laevis oocytes was ...
    • Ion Permeation of AQP6 Water Channel Protein: Single-Channel Recordings After Hg2+ Activation 

      Guggino, William B.; Hazama, Akihiro; Kozono, David; Yasui, Masato; Agre, Peter (American Society for Biochemistry and Molecular Biology, 2002-08-09)
      Aquaporin-6 (AQP6) has recently been identified as an intracellular vesicle water channel with anion permeability that is activated by low pH or HgCl2. Here we present direct evidence of AQP6 channel gating using patch ...
    • Membrane topology of aquaporin CHIP. Analysis of functional epitope-scanning mutants by vectorial proteolysis 

      Jung, Jin S.; Preston, Gregory M.; Agre, Peter; Guggino, William B. (American Society for Biochemistry and Molecular Biology, 1994-01-21)
      CHIP is the archetypal member of the aquaporins, a widely expressed family of membrane water channels. The NH2- and COOH-terminal halves of CHIP are sequence-related, and hydropathy analysis predicted six membrane-spanning ...
    • The mercury-sensitive residue at cysteine 189 in the CHIP28 water channel 

      Jung, Jin Sup; Preston, Gregory M.; Agre, Peter; Guggino, William B. (American Society for Biochemistry and Molecular Biology, 1993-01-05)
      Water channels provide the plasma membranes of red cells and renal proximal tubules with high permeability to water, thereby permitting water to move in the direction of an osmotic gradient. Molecular identification of ...
    • Molecular characterization of an aquaporin cDNA from brain: candidate osmoreceptor and regulator of water balance 

      Agre, Peter; Baraban, Jay M.; Guggino, William B.; Preston, Gregory M.; Bhat, Ratan V.; Jung, Jin Sup (National Academy of Sciences, 1994-12-20)
      The aquaporins transport water through membranes of numerous tissues, but the molecular mechanisms for sensing changes in extracellular osmolality and regulating water balance in brain are unknown. We have isolated a brain ...
    • 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, ...
    • Molecular cloning and characterization of AqpZ, a water channel from Escherichia coli 

      Bishai, William R.; Guggino, William B.; Agre, Peter; Preston, Gregory M.; Calamita, Giuseppe (American Society for Biochemistry and Molecular Biology, 1995-12-08)
      The aquaporin family of molecular water channels is widely expressed throughout the plant and animal kingdoms. No bacterial aquaporins are known; however, sequence-related bacterial genes have been identified that encode ...
    • Molecular struture of the water channel through aquaporin CHIP. The hourglass model. 

      Smith, Barbara L.; Jung, Jin Sup; Preston, Gregory M.; Agre, Peter; Guggino, William B. (American Society for Biochemistry and Molecular Biology, 1994-05-20)
      Aquaporin channel-forming integral protein (CHIP) is the first characterized water channel protein (genome symbol AQP1), but the molecular structure of the aqueous pathway through CHIP remains undefined. The two halves of ...
    • Water channel properties of major intrinsic protein of lens 

      Agre, Peter; Van Os, Carel H.; Guggino, William B.; Deen, Peter M. T.; Preston, Gregory M.; Mulders, Sabine M. (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. ...