P
Peter Agre
Researcher at Johns Hopkins University
Publications - 250
Citations - 41145
Peter Agre is an academic researcher from Johns Hopkins University. The author has contributed to research in topics: Aquaporin & Aquaporin 1. The author has an hindex of 104, co-authored 248 publications receiving 39051 citations. Previous affiliations of Peter Agre include GlaxoSmithKline & Aarhus 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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Structural determinants of water permeation through aquaporin-1.
Kazuyoshi Murata,Kaoru Mitsuoka,Teruhisa Hirai,Thomas Walz,Peter Agre,J. B. Heymann,Andreas Engel,Yoshinori Fujiyoshi +7 more
TL;DR: An atomic model of human red cell AQP1 is described, providing a possible molecular explanation to a longstanding puzzle in physiology—how membranes can be freely permeable to water but impermeable to protons.
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Specialized membrane domains for water transport in glial cells : high-resolution immunogold cytochemistry of aquaporin-4 in rat brain
Søren Nielsen,Erlend A. Nagelhus,Mahmood Amiry-Moghaddam,Charles W. Bourque,Peter Agre,Ole Petter Ottersen +5 more
TL;DR: The highly polarized AQP4 expression indicates that these cells are equipped with specific membrane domains that are specialized for water transport, thereby mediating the flow of water between glial cells and the cavities filled with CSF and the intravascular space.
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Aquaporins in the Kidney: From Molecules to Medicine
TL;DR: In conditions with water retention such as severe congestive heart failure, pregnancy, and syndrome of inappropriate antidiuretic hormone secretion, both AQP 2 expression levels and apical plasma membrane targetting are increased, suggesting a role for AQP2 in the development of water retention.
Journal ArticleDOI
Aquaporin water channels – from atomic structure to clinical medicine
Peter Agre,Landon S. King,Masato Yasui,Wm B. Guggino,Ole Petter Ottersen,Yoshinori Fujiyoshi,Andreas Engel,Søren Nielsen +7 more
TL;DR: The water permeability of biological membranes has been a longstanding problem in physiology, but the proteins responsible for this remained unknown until discovery of the aquaporin 1 (AQP1) water channel protein.