نتایج جستجو برای: aquaporin 1

تعداد نتایج: 2756237  

Journal: :Journal of molecular biology 2000
B L de Groot J B Heymann A Engel K Mitsuoka Y Fujiyoshi H Grubmüller

The fold of human aquaporin 1 is determined from cryo-electron microscopic data at 4.5 A resolution. The monomeric structure consists of two transmembrane triple helices arranged around a pseudo-2-fold axis connected by a long flexible extracellular loop. Each triplet contains between its second and third helix a functional loop containing the highly conserved fingerprint NPA motif. These funct...

Journal: :ACS chemical biology 2013
Daniel Seeliger Cinta Zapater Dawid Krenc Rose Haddoub Sabine Flitsch Eric Beitz Joan Cerdà Bert L de Groot

Human aquaporin-1 (hAQP1) is a water channel found in many tissues and potentially involved in several human pathologies. Selective inhibitors of hAQP1 are discussed as novel treatment opportunities for glaucoma, brain edema, inflammatory pain, and certain types of cancer. However, only very few potent and chemically attractive blockers have been reported to date. In this study we present three...

2016
Janet To Jaume Torres

Aquaporins (AQPs) are membrane proteins that enable water transport across cellular plasma membranes in response to osmotic gradients. Phenotypic analyses have revealed important physiological roles for AQPs, and the potential for AQP water channel modulators in various disease states has been proposed. For example, AQP1 is overexpressed in tumor microvessels, and this correlates with higher me...

Background: Among aflatoxins, the subtype aflatoxin G1 is one of the most toxic, commonly found in cereals, legumes, dairy and non-alcoholic beers. Aflatoxins have been known as nephrotoxic compounds. In this study, changes in the expression of aquaporin-1, the histopathology of renal tissue and plasma biochemical factors after exposure to aflatoxin G1 were investigated in mice. Methods: Twent...

Journal: :Journal of molecular biology 2007
Hector Viadiu Tamir Gonen Thomas Walz

Aquaporin-9, an aquaglyceroporin present in diverse tissues, is unique among aquaporins because it is not only permeable to water, urea and glycerol, but also allows passage of larger uncharged solutes. Single particle analysis of negatively stained recombinant rat aquaporin-9 revealed a particle size characteristic of the tetrameric organization of all members of the aquaporin family. Reconsti...

2015
Ying Hsu Minh Tran Andreas A. Linninger

Aquaporin-4 water channels play a central role in brain water regulation in neurological disorders. Aquaporin-4 is abundantly expressed at the astroglial endfeet facing the cerebral vasculature and the pial membrane, and both its expression level and subcellular localization significantly influence brain water transport. However, measurements of aquaporin-4 levels in animal models of brain inju...

2013
Letizia Mezzasoma Lucio Cagini Cinzia Antognelli Francesco Puma Eugenio Pacifico Vincenzo Nicola Talesa

Postoperative-fluid retention is a severe complication frequently reported in patients undergoing major surgical procedures. The complex network of molecules involved in such a severe surgery-induced condition remains poorly understood. Inflammation has been proposed among the various causes of fluid retention. Since TNF-α is one of the main proinflammatory cytokine initially released after maj...

2014
Douglas Kazutoshi Sato Dagoberto Callegaro Frederico M de Haidar Jorge Ichiro Nakashima Shuhei Nishiyama Toshiyuki Takahashi Renata Faria Simm Samira Luisa Apostolos-Pereira Tatsuro Misu Lawrence Steinman Masashi Aoki Kazuo Fujihara

To elucidate immunopathogenetic roles of aquaporin-4 antibodies in the cerebrospinal fluid (CSF) of neuromyelitis optica spectrum disorders (NMOSD), we analyzed aquaporin-4 antibody titers, cellular and inflammatory markers in the CSF collected from 11 aquaporin-4 antibody seropositive patients. The CSF aquaporin-4 antibody levels during attacks (but not in sera) closely correlated with pleocyt...

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