Search for dissertations about: "aquaporin 1"
Showing result 1 - 5 of 36 swedish dissertations containing the words aquaporin 1.
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1. Expression and Function of Human and Plant Aquaporins
Abstract : The aquaporins (AQPs) belong to a family of water permeable membrane channels found in virtually all living organisms. Thirteen isoforms of mammalian AQPs are found, whereas in Arabidopsis thaliana 35 genes encoding AQPs are found. The AQPs are distributed in different organs, cell types and in different subcellular membranes. READ MORE
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2. Regulation of glycerol efflux in adipocytes. Structural and functional studies of the glycerol channel aquaporin 7
Abstract : Glycerol levels in adipocytes depend on the lipolysis, the hydrolysis of triglycerides into glycerol and free fatty acids, and the efflux of glycerol across the plasma membrane through glycerol channels. The aims of this work were to investigate how glycerol levels are regulated on a molecular level by PLIN1, a major lipid droplet-associated protein and a key regulator of the lipolysis by scaffolding for lipolytic proteins on the lipid droplet. READ MORE
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3. Plant aquaporin regulation: Structural and functional studies using diffraction and scattering techniques
Abstract : Water is the basis for life as we know it. It is only logical then that all organisms have evolved specialized proteins, aquaporins, which regulate water flow across their membranes. Plants, which are immobile, depend more on their environment and also use water flows to move, to breathe, and to grow. READ MORE
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4. A Holistic View on Aquaporins: Production, Structure, Function and Interactions
Abstract : Aquaporins are specialised membrane proteins, which regulate the water homeostasis of cells. In eukaryotic organisms, this process is tightly regulated, and aberrations in aquaporin functionality lead to severe pathologies in humans. READ MORE
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5. Marginally hydrophobic transmembrane α-helices shaping membrane protein folding
Abstract : Most membrane proteins are inserted into the membrane co-translationally utilizing the translocon, which allows a sufficiently long and hydrophobic stretch of amino acids to partition into the membrane. However, X-ray structures of membrane proteins have revealed that some transmembrane helices (TMHs) are surprisingly hydrophilic. READ MORE