Julie Winkel Missel
Gæsteforsker
Molecular Cardiology and Membrane Proteins
Blegdamsvej 3
2200 København N.
My research aims to characterize the structural and functional mechanisms of human aquaporins (AQPs). AQPs are water transporting pores engulfed in the plasma membrane of the cells. AQPs can be divided into three subgroups: orthodox AQPs, aquaglyceroporins, and super AQPs. The orthodox AQPs consist of AQP0,1,2,4,5,6 and 8 and are responsible for simple water transport. The aquaglyceroporins consist of AQP3,7,9 and 10, which, besides water, are also responsible for glycerol transport among other small solutes. Lastly, the super AQPs share low sequence similarity to the other AQPs, and their function and mechanism are today the least investigated of the three subgroups, while only minimal functional data has been published. To date orthodox AQPs have been extensively investigated, but zero structures of the human aquaglyceroporins and super AQPs have been reported.
ID: 162967641
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Purification and functional comparison of nine human Aquaporins produced in Saccharomyces cerevisiae for the purpose of biophysical characterization
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Structure of the human ClC-1 chloride channel
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Human adipose glycerol flux is regulated by a pH gate in AQP10
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