Sandra Pacharra

TL;DR: Glycopeptide analysis by liquid chromatography-tandem mass spectrometry allowed for the identification of some of the O-mannosylation sites, which were not restricted to the mucin domain but were found also within N-terminal IgG and Fibronectin domains of the protein.

TL;DR: By fractionating and analyzing the glycoproteome of mouse and calf brain lysates, it is shown that proteins of the perineural net, the lecticans, are O-mannosylated, indicating that major components of neuronal extracellular matrix are O -mannosyated in mammalian brain.

TL;DR: Structural evidence is provided for a novel type of mucin-type O-glycans that is strictly specific for LacdiNAc termini: sugar phosphorylation with formation of GalNAcβ1–4(phospho-)GlcNAc.

TL;DR: A Gel-based global O-glycomics method applicable for highly complex protein mixtures entrapped in discontinuous gradient gel layers that offers robust performance with sensitivity in the low picomolar range, is compatible with gel-based proteomics, and shows superior performance in global applications in comparison with workflows eliminating glycans in-gel or from electroblotted glycoproteins.

TL;DR: Perez-Riverol et al. as mentioned in this paper presented a data dependent acquisition (DDA) dataset which was generated as a reference and ground truth quantitative dataset, which consists of 15 LC-MS/MS measurements composed of five distinct spike-in-states, each with three replicates.