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Fredrik Öberg

Researcher at University of Gothenburg

Publications -  15
Citations -  663

Fredrik Öberg is an academic researcher from University of Gothenburg. The author has contributed to research in topics: Membrane protein & Pichia pastoris. The author has an hindex of 10, co-authored 15 publications receiving 577 citations. Previous affiliations of Fredrik Öberg include Chalmers University of Technology.

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X-ray structure of human aquaporin 2 and its implications for nephrogenic diabetes insipidus and trafficking

TL;DR: The X-ray structure of human AQP2 is presented and the locations of several NDI-causing mutations can be observed, primarily situated within transmembrane domains and the majority of which cause misfolding and ER retention, to provide a framework for understanding why mutations in AQp2 cause NDI.
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CO2 permeability of cell membranes is regulated by membrane cholesterol and protein gas channels

TL;DR: The gas permeability of membranes for the case of CO2 is studied using a previously established mass spectrometric technique, indicating that gas channels are of high functional significance for gas transfer across membranes of low intrinsicGas permeability.
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Exceptional overproduction of a functional human membrane protein

TL;DR: The power of the yeast P. pastoris as a host to produce exceptionally high yields of a functionally active, human integral membrane protein for subsequent functional and structural characterization is illustrated.
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A Lipidic-Sponge Phase Screen for Membrane Protein Crystallization

TL;DR: A sparse matrix crystallization screen consisting of 48 lipidic-sponge phase conditions and how the screen may be manipulated by incorporating specific lipids such as cholesterol is demonstrated; this modification led to crystals being recovered from a bacterial photosynthetic core complex.
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Glycosylation Increases the Thermostability of Human Aquaporin 10 Protein

TL;DR: Overproduced hAQP10 in the yeast Pichia pastoris is overproduced and it is observed that the protein is glycosylated at Asn-133 in the extracellular loop C, which confirms one of three predicted Glycosylation sites for hA QP10, and its gly cosylation is unique for the human aquaporins overproduced in this host.