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- W4318615673 startingPage "15" @default.
- W4318615673 abstract "Aquaporins (AQPs) allow water molecules and other small, neutral solutes to quickly pass through membrane. The protein structures of AQPs solved by crystallographic methods or cryo-electron microscopy technology show that AQP monomer consists of six membrane-spanning alpha-helices that form the central water-transporting pore. AQP monomers assemble to form tetramers, forming the functional units in the membrane, to transport water or other small molecules. The biological functions of AQPs are regulated by posttranslational modifications, e.g., phosphorylation, ubiquitination, glycosylation, subcellular distribution, degradation and protein interactions. Modifications of AQP combined with structural properties contribute to a better functional mechanism of AQPs. Insight into the molecular mechanisms responsible for AQP modifications as well as gating and transport properties proved to be fundamental to the development of new therapeutic targets or reliable diagnostic and prognostic biomarkers." @default.
- W4318615673 created "2023-01-31" @default.
- W4318615673 creator A5015849291 @default.
- W4318615673 creator A5047894137 @default.
- W4318615673 creator A5071615222 @default.
- W4318615673 creator A5082063789 @default.
- W4318615673 date "2023-01-01" @default.
- W4318615673 modified "2023-10-17" @default.
- W4318615673 title "Protein Structure and Modification of Aquaporins" @default.
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