Glycosylation, the covalent attachment of simple or complex sugar structures onto proteins, is the most abundant post-translational modification in biology. Over 50% of human proteins are subject to these dynamic modifications, which alter their activities in fundamental biological processes, such as cell adhesion, nuclear transport, signal transduction, intracellular trafficking, protein localization, host-pathogen interactions, or essential immune functions.
To identify and functionally validate the role of glycoproteins in complex biological systems, we developed a novel quantitative approach to isolate intact glycopeptides from comparative proteomic data-sets. This approach allows us to not only infer complex sugar structures, but to also directly map them to sites within the associated proteins at the proteome scale. This novel comparative and high-throughput glycoproteomics platform enables genome-wide insights into protein glycosylation and sugar modifications.
SugarQb is a collection of software tools (Nodes) which enable the automated identification of intact glycopeptides from HCD‐MS/MS data sets, using commonly use peptide-centric MS/MS search engines (e.g. MASCOT, SEQUEST‐HT) in the Proteome Discoverer 1.4 environment.
SugarQb is freely available to all researchers.
For further information on the algorithm, please refer to the corresponding publication Stadlmann J., Taubenschmid J., et al. Comparative glycoproteomics of stem cells identifies new players in ricin toxicity, Nature (2017).
HAPLOBANK is a collection of 100,000 individual haploid murine embryonic stem cell lines targeting 16,950 genes which can be used to functionally validate high-throughput screening candidates or to study in-depth phenotypic effects of gene loss, not only in ES cells, but also into various differentiated cell types.
A necessary and indispensable tool to understand complex human disease is the generation and study of genetic mouse models. Please find in the Excel sheets the mouse lines as well as Cre-expressing lines available in the lab. We kindly acknowledge the helpful collaboration of other research groups who provided some of these lines.