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Michael Mormann

Researcher at University of Münster

Publications -  55
Citations -  1259

Michael Mormann is an academic researcher from University of Münster. The author has contributed to research in topics: Mass spectrometry & Shiga toxin. The author has an hindex of 22, co-authored 54 publications receiving 1119 citations. Previous affiliations of Michael Mormann include Bielefeld University.

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Elucidation of glycoprotein structures by unspecific proteolysis and direct nanoESI mass spectrometric analysis of ZIC-HILIC-enriched glycopeptides.

TL;DR: The presented method is a fast, facile, and inexpensive procedure for the elucidation of protein N-glycosylation and the glycopeptides produced by the above proteases contain short peptide backbones thus improving-probably due to their higher hydrophilicity--the ZIC-HILIC-based separation.
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Dystroglycan binding to α-neurexin competes with neurexophilin-1 and neuroligin in the brain.

TL;DR: Expression of αDAG and Nxph1 together with alternative splicing in Nrxn1α may prevent or facilitate formation of distinct trans-synaptic N Rxn·Nlgn complexes, revealing an unanticipated way to contribute to the identity of synaptic subpopulations.
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Promiscuous Shiga toxin 2e and its intimate relationship to Forssman

TL;DR: These findings provide a basis for further exploring the functional role of the promiscuous receptor repertoire of Stx2e and the exact nature of the mechanisms that underlie different pathological outcomes of StX2e-producing STEC in humans and pigs.
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Thin-layer chromatography, overlay technique and mass spectrometry: a versatile triad advancing glycosphingolipidomics.

TL;DR: It is believed that the combinatorial approach using conventional TLC and modern mass spectrometry provides a developmental advance in exploring the glycosphingolipidome of biological material.
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Fragmentation of intra-peptide and inter-peptide disulfide bonds of proteolytic peptides by nanoESI collision-induced dissociation

TL;DR: Results on the fragmentation of intra and inter-peptide disulfide bonds of proteolytic peptides by nano electrospray ionisation collision-induced dissociation (nanoESI CID) are shown.