Scheduled Maintenance Alert:
To start on September 25th @ 9:30 EST, we will be performing a server upgrade. During this time, you may experience brief interruptions in service. We apologize for any inconvenience and appreciate your patience as we work to enhance our platform.
JScholarship will not be available during the upgrade window but which is expected to last for 1 hour but could take much longer.
Peter Agre
Browse by
Dr. Peter Agre, 2003 Nobel Prize winner in chemistry, is currently the director of the Johns Hopkins Malaria Research Institute. In addition to the Nobel Prize, Dr. Agre's honors include election to the National Academy of Sciences in 2000, the Institute of Medicine in 2005, the American Academy of Arts and Sciences in 2003, and the American Philosophical Society in 2004.
Dr. Agre's research in red-blood-cell biochemistry led to the first known membrane defects in congenital hemolytic anemias (spherocytosis) and produced the first isolation of the Rh blood group antigens. In 1992, his laboratory became widely recognized for discovering the aquaporins, a family of water channel proteins found throughout nature and responsible for numerous physiological processes in humans— including kidney concentration, as well as secretion of spinal fluid, aqueous humor, tears, sweat, and release of glycerol from fat.
Dr. Agre's research in red-blood-cell biochemistry led to the first known membrane defects in congenital hemolytic anemias (spherocytosis) and produced the first isolation of the Rh blood group antigens. In 1992, his laboratory became widely recognized for discovering the aquaporins, a family of water channel proteins found throughout nature and responsible for numerous physiological processes in humans— including kidney concentration, as well as secretion of spinal fluid, aqueous humor, tears, sweat, and release of glycerol from fat.
Recent Submissions
-
Man is not a rodent: aquaporins in the airways
(American Thoracic Society, 2001-03) -
Respiratory aquaporins in lung inflammation: the night is young
(American Thoracic Society, 2000-01) -
Linkage of dominant hereditary spherocytosis to the gene for the erythrocyte membrane-skeleton protein ankyrin
(Massachusetts Medical Society, 1990-10-11) -
Aquaporin water channels [Nobel Lecture]
(Gesellschaft Deutscher Chemiker, 2004) -
Defective cellular trafficking of lacrimal gland aquaporin-5 in Sjögren's syndrome
(Elsevier, 2001-06-23)Dry eyes and dry mouth are clinical hallmarks of Sjögren's syndrome. We assessed the distribution of aquaporin-5 (AQP5) in lacrimal gland biopsy samples. Healthy controls and patients with Mikulicz's disease or non-Sjögren's ... -
Aquaporins in complex tissues. I. Developmental patterns in respiratory and glandular tissues of rat
(American Physological Society, 1997-11)Developmental expression of aquaporin water transport proteins is not well understood in respiratory tract or secretory glands; here we define aquaporin protein ontogeny in rat. Expression of aquaporin-3 (AQP3), AQP4, and ... -
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 ... -
Mutations in aquaporin-1 in phenotypically normal humans without functional CHIP water channels
(American Association for the Advancement of Science, 1994-09-09)The gene aquaporin-1 encodes channel-forming integral protein (CHIP), a member of a large family of water transporters found throughout nature. Three rare individuals were identified who do not express CHIP-associated ... -
Structural determinants of water permeation through aquaporin-1
(Nature Publishing Group, 2000-10-05)Human red cell AQP1 is the first functionally defined member of the aquaporin family of membrane water channels. Here we describe an atomic model of AQP1 at 3.8A resolution from electron crystallographic data. Multiple ... -
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 ... -
Appearance of Water Channels in Xenopus Oocytes Expressing Red Cell CHIP28 Protein
(American Association for the Advancement of Science, 1992-04-17)Water rapidly crosses the plasma membrane of red blood cells (RBCs) and renal tubules through specialized channels. Although selective for water, the molecular structure of these channels is unknown. The CHIP28 protein is ... -
Partial deficiency of erythrocyte spectrin in hereditary spherocytosis.
(Nature Publishing Group, 1985-03-28)Hereditary spherocytosis (HS) is a common, clinically heterogeneous haemolytic anaemia in which the primary erythrocyte defect is believed to be some abnormality in the spectrin-actin membrane skeleton, leading to loss of ... -
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 ... -
Reconstitution of functional water channels in liposomes containing purified red cell CHIP28 protein
(American Chemical Society, 1992) -
Inheritance pattern and clinical response to splenectomy as a reflection of erythrocyte spectrin deficiency in hereditary spherocytosis
(Massachusetts Medical Society, 1986-12-18)To determine how various inheritance patterns and responses to splenectomy relate to erythrocyte spectrin deficiencies in hereditary spherocytosis, we measured the spectrin content of erythrocytes by radioimmunoassay in ... -
Deficient red-cell spectrin in severe, recessively inherited spherocytosis
(Massachusetts Medical Society, 1982-05-13) -
The Rh polypeptide is a major fatty acid-acylated erythrocyte membrane protein
(American Society for Biochemistry and Molecular Biology, 1988-12-05)The erythrocyte Rh antigens contain an Mr = 32,000 integral protein which is thought to contribute in some way to the organization of surrounding phospholipid. To search for possible fatty acid acylation of the Rh polypeptide, ... -
Water and ion permeation of aquaporin-1 in planar lipid bilayers. Major differences in structural determinants and stoichiometry.
(American Society for Biochemistry and Molecular Biology, 2001-08-24)The aquaporin-1 (AQP1) water channel protein is known to facilitate the rapid movement of water across cell membranes, but a proposed secondary role as an ion channel is still unsettled. Here we describe a method to ... -
Functional expression and characterization of an archaeal aquaporin. AqpM from methanothermobacter marburgensis.
(American Society for Biochemistry and Molecular Biology, 2003-03-21)Researchers have described aquaporin water channels from diverse eubacterial and eukaryotic species but not from the third division of life, Archaea. Methanothermobacter marburgensis is a methanogenic archaeon that thrives ... -
Characterization of aquaporin-6 as a nitrate channel in mammilian cells: Requirement of pore-lining residue threonine 63
(American Society for Biochemistry and Molecular Biology, 2002-10-18)Aquaporins (AQP) were originally regarded as plasma membrane channels that are freely permeated by water or small uncharged solutes but not by ions. Unlike other aquaporins, AQP6 overexpressed in Xenopus laevis oocytes was ...
RSS 1.0