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Molecular characterization of an aquaporin cDNA from brain: candidate osmoreceptor and regulator of water balance
(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 ...
The mercury-sensitive residue at cysteine 189 in the CHIP28 water channel
(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 struture of the water channel through aquaporin CHIP. The hourglass model.
(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 ...
The human AQP4 gene: definition of the locus encoding two water channel polypeptides in brain
(National Academy of Sciences, 1996-10-01)
The aquaporin family of membrane water transport proteins are expressed in diverse tissues, and in brain the predominant water channel protein is AQP4. Here we report the isolation and characterization of the human AQP4 ...