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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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    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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    Developmental gene expression and tissue distribution of the CHIP28 water-channel protein 

    Agre, Peter; Preston, Gregory M.; Smith, Barbara L.; Chin, Edward; Bondy, Carolyn (National Academy of Sciences, 1993-05-15)
    The CHIP28 water channel is a major component of red cell and renal tubule membranes; however, its ontogeny and tissue distribution remain undefined. Three patterns of expression were identified when CHIP28 mRNA was surveyed ...
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    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 ...
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    The human aquaporin-CHIP gene. Structure, organization, and chromosomal localization 

    Agre, Peter; Jabs, Ethylin Wang; Griffin, Constance A.; Preston, Gregory M.; Moon, Chulso (American Society for Biochemistry and Molecular Biology, 1993-07-25)
    Aquaporin-CHIP is the first known molecular water channel. Originally identified in red cells and renal tubules, transcripts and proteins related to AQP-CHIP are also expressed in diverse epithelia with distinct developmental ...
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    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 ...
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    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 ...
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    Isolation of the cDNA for erythrocyte integral membrane protein of 28 kilodaltons: member of an ancient channel family 

    Agre, Peter; Preston, Gregory M. (National Academy of Sciences, 1991-12-15)
    CHIP28 is a 28-kDa integral membrane protein with similarities to membrane channels and is found in erythrocytes and renal tubules. A cDNA for CHIP28 was isolated from human fetal liver cDNA template by a three-step ...
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    Functional analysis of aquaporin-1 deficient red cells 

    Mori, Susumu; Mathai, John C.; Preston, Gregory M.; Smith, Barbara L. (American Society for Biochemistry and Molecular Biology, 1996-01-19)
    The aquaporin-1 (AQP1) water transport protein contains a polymorphism corresponding to the Colton red blood cell antigens. To define the fraction of membrane water permeability mediated by AQP1, red cells were obtained ...
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    Preston, Gregory M. (16)
    Agre, Peter (15)Guggino, William B. (8)Smith, Barbara L. (5)Jung, Jin Sup (3)Anstee, David J. (2)Griffin, Constance A. (2)Raina, Surabhi (2)Baraban, Jay M. (1)Baumgarten, Ruben (1)... View MoreSubjectAquaporins (15)Ion Channels/genetics (3)Water/metabolism (3)Erythrocytes/physiology (2)Ion Channels/biosynthesis (2)Ion Channels/chemistry (2)Membrane Proteins/genetics (2)Oocytes/physiology (2)ABO Blood-Group System/chemistry (1)Anemia (1)... View MoreDate Issued1994 (5)1993 (4)1995 (3)1996 (2)1991 (1)1992 (1)Has File(s)Yes (16)

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