G
Gregory M. Preston
Researcher at Pfizer
Publications - 45
Citations - 8162
Gregory M. Preston is an academic researcher from Pfizer. The author has contributed to research in topics: Aquaporin 1 & Aquaporin. The author has an hindex of 26, co-authored 44 publications receiving 7775 citations. Previous affiliations of Gregory M. Preston include Johns Hopkins University School of Medicine & Johns Hopkins University.
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Appearance of water channels in Xenopus oocytes expressing red cell CHIP28 protein.
TL;DR: Oocytes from Xenopus laevis microinjected with in vitro-transcribed CHIP28 RNA exhibited increased osmotic water permeability; this was reversibly inhibited by mercuric chloride, a known inhibitor of water channels, so it is likely that ChIP28 is a functional unit of membrane water channels.
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Isolation of the cDNA for erythrocyte integral membrane protein of 28 kilodaltons: member of an ancient channel family.
Gregory M. Preston,Peter Agre +1 more
TL;DR: Analysis of the deduced amino acid sequence suggests that CHIP28 protein contains six bilayer-spanning domains, two exofacial potential N-glycosylation sites, and intracellular N and C termini.
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Molecular characterization of an aquaporin cDNA from brain: candidate osmoreceptor and regulator of water balance
TL;DR: Its distinctive expression pattern implicates this fourth mammalian member of the aquaporin water channel family (designated gene symbol, AQP4) as the osmoreceptor which regulates body water balance and mediates water flow within the central nervous system.
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Aquaporin CHIP: the archetypal molecular water channel
Peter Agre,Gregory M. Preston,Barbara L. Smith,Jin Sup Jung,Surabhi Raina,Chulso Moon,William B. Guggino,Søren Nielsen +7 more
TL;DR: Recognition of CHIP has provided molecular insight into the biological phenomenon of osmotic water movement, and it is hoped that pharmacological modulation ofCHIP function may provide novel treatments of renal failure and other clinical problems.
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Molecular structure of the water channel through aquaporin CHIP. The hourglass model.
TL;DR: An hourglass structural model is proposed in which a cytoplasmic chamber connects within the membrane to an extracellular chamber (loop E) forming a single, narrow aqueous pathway through each of the CHIP subunits; subunit oligomerization may provide the vertical symmetry necessary for residence within the lipid bilayer.