Results 271 to 280 of about 66,082 (286)
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Renal expression and functions of aquaporin 1 and aquaporin 4 in cattle
Biotechnic & Histochemistry, 2013Aquaporin (AQP) 1 and AQP 4 are members of the aquaporin water channel family that play an important role in reabsorption of water from the renal tubular fluid to concentrate urine. Studies of renal AQPs have been performed in human, rodents, sheep, dogs and horses.
K, Altunbas +3 more
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Aquaporin-1 Antibody in Neuromyelitis Optica Patients
European Neurology, 2014<b><i>Background/Methods:</i></b> To find out the prevalence of aquaporin-antibody (Aqp-Ab) and characterize Aqp-Ab associated clinical features in NMO, Aqp-1 and Aqp-4-Abs were examined using radioimmunoprecipitation and cell-based assays, respectively.
Erdem, Tüzün +10 more
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Aquaporin 1 expression in human temporomandibular disc
Acta Histochemica, 2012Aquaporins (AQPs) are a family of hydrophobic membrane channel proteins. The expression of several AQP isoforms has been investigated in different human tissues, including the orofacial region. However, information on the role and localization of AQP1 in joints is limited, and no data are available on aquaporins in the normal temporomandibular joint ...
LORETO, CARLA AGATA +8 more
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The three-dimensional structure of aquaporin-1
Nature, 1997The 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 in Xenopus oocytes and functional studies of an erythrocyte integral membrane protein of relative molecular mass 28,000 ...
Engel, Andreas +8 more
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Aquaporins in complex tissues: distribution of aquaporins 1–5 in human and rat eye
American Journal of Physiology-Cell Physiology, 1998Multiple physiological fluid movements are involved in vision. Here we define the cellular and subcellular sites of aquaporin (AQP) water transport proteins in human and rat eyes by immunoblotting, high-resolution immunocytochemistry, and immunoelectron microscopy.
Hamann, Steffen +6 more
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Identification of Aquaporin 1 in Diplodus sargus
2013Aquaporin 1 (AQP-1) is the first member of the aquaporin family, which includes seven homologs in teleosts, involved in the selective transport of water, small neutral molecules, and ions. AQPs contain six transmembrane helices, five connecting loops, and the amino and carboxyl ends protrude into the cytoplasm.
Zanghi' G. +4 more
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Selective Permeability of Truncated Aquaporin 1 in Silico
ACS Biomaterials Science & Engineering, 2017Aquaporin (AQP) proteins function as highly efficient water transport channels that support homeostasis in many types of living cells. Their structure-function relationships have been characterized extensively in fundamental and applied research, primarily via structural analysis, mutational studies, and computational approaches.
Karl Decker +5 more
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Diagnostic significance of aquaporin-1 in liver tumors
Human Pathology, 2005The diagnostic utility of aquaporin (AQP)-1 in liver tumors was tested and compared with other well-established markers. In 30 cholangiocarcinomas (CCs), 20 hepatocellular carcinomas (HCCs), and 10 metastatic colorectal carcinomas (MCCs) of the liver, expression of AQP-1, CD10, cytokeratin (CK) 7, CK20, and polyclonal carcinoembryonic antigen (pCEA ...
Peter R, Mazal +3 more
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Length of the selectivity filter of aquaporin‐1*
Biology of the Cell, 1997We have characterized the selectivity filter of the water channel aquaporin‐1 (AQP1) of proximal straight tubules (PST), as an equivalent cylindrical structure with a diameter of ∼ 4.5 Å, where water molecules single file. We report here efforts to evaluate its length.
G, Whittembury +4 more
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Structural determinants of water permeation through aquaporin-1
Nature, 2000Human 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 highly conserved amino-acid residues stabilize the novel fold of AQP1. The aqueous pathway is lined with conserved hydrophobic residues
Murata, K. +7 more
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