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The human Aquaporin-5 gene. Molecular characterization and chromosomal localization.
(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) ...
Quantification of Aquaporin-CHIP water channel protein in microdissected renal tubules by fluorescence-based ELISA
(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 ...
Molecular analysis of insertion/deletion mutations in protein 4.1 in elliptocytosis. II. Determination of molecular genetic origins of rearrangements
(American Society for Clinical Investigation, 1990-08)
Protein 4.1 is an approximately 80-kD structural protein in the membrane skeleton which underlies and supports the erythrocyte plasma membrane. The preceding companion paper presents a biochemical study of two abnormal ...
The mouse telomerase RNA 5"-end lies just upstream of the telomerase template sequence
(Oxford University Press, 1998-01-15)
Telomerase is a ribonucleoprotein enzyme with an essential RNA component. Embedded within the telomerase RNA is a template sequence for telomere synthesis. We have characterized the structure of the 5' regions of the human ...
Erythrocyte Mr 28,000 transmembrane protein exists as a multisubunit oligomer silimar to channel proteins
(American Society for Biochemistry and Molecular Biology, 1991-04-05)
A novel Mr 28,000 erythrocyte transmembrane protein was recently purified and found to exist in two forms, "28kDa" and "gly28kDa," the latter containing N-linked carbohydrate (Denker, B. M., Smith, B. L., Kuhajda, F. P., ...
Heterotetrameric composition of aquaporin-4 water channels.
(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 ...
Rapid gating and anion permeability of an intracellular aquaporin
(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 ...
Reconstitution of functional water channels in liposomes containing purified red cell CHIP28 protein
(American Chemical Society, 1992)
Aquaporin-4 water channel protein in the rat retina and optic nerve: polarized expression in Müller cells and fibrous astrocytes
(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 ...
The three-dimensional structure of aquaporin-1
(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 ...