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Joerg Hoernschemeyer

Researcher at University of Bonn

Publications -  9
Citations -  1071

Joerg Hoernschemeyer is an academic researcher from University of Bonn. The author has contributed to research in topics: Recombinant DNA & Glycoprotein. The author has an hindex of 7, co-authored 9 publications receiving 1003 citations.

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Proteomic and biochemical analyses of human B cell-derived exosomes. Potential implications for their function and multivesicular body formation.

TL;DR: Data suggest that recruitment of membrane proteins from the limiting membranes into the internal vesicles of multivesicular bodies may involve their incorporation into tetraspanin-containing detergent-resistant membrane domains.
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Human acid sphingomyelinase - Assignment of the disulfide bond pattern

TL;DR: The hypothesis that haSMase possesses an intramolecular SAP-type activator domain as predicted by sequence comparison is supported and an additional analysis of ha SMase isolated from human placenta shows that the recombinant and the native human protein possess an identical disulfide structure.
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Photoaffinity labelling of the human GM2-activator protein: Mechanistic insight into ganglioside GM2 degradation

TL;DR: Results provide strong evidence that the hydrophobicity and the great structural mobility of this element are crucial for the extraction of the membrane-embedded glycolipid, its stabilization inside the spacious cavity and its guidance to the enzyme's active site.
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Expression of recombinant human GM2-activator protein in insect cells: purification and characterization by mass spectrometry.

TL;DR: The biological activity of the recombinant protein was demonstrated by its ability to stimulate the hexosaminidase A-catalyzed degradation of ganglioside GM2, and the homogeneity and glycosylation were assessed by ESI-TOF mass spectrometry.
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Expression of the GM2-activator protein in the methylotrophic yeast Pichia pastoris, purification, isotopic labeling, and biophysical characterization.

TL;DR: A convenient eukaryotic system that allows the efficient production of functionally folded, glycosylated GM2AP and offers the potential of cost-efficient isotopic labeling for structural studies by NMR spectroscopy is established.