Novel MS Based Proteomics Technologies

Maarten Altelaar develops and implements novel MS based proteomics technologies to study protein regulation and cellular signaling processes. Emphasis lies on neuronal cell differentiation and cancer signaling in acquired drug resistance and immune therapy. High-throughput (phospho)proteomics complemented with top-down MS technologies are used to target proteome dynamics


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We're happy to welcome Kelly Stecker as new postdoc in the group

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We're happy to welcome Charlotte van Gelder as a new PhD student in the group

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PhosphoPath available via the Cytoscape app store

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Congratulations to Ana Guerreiro who successfully defended her PhD on 11th January 2016


Congratulations to Donna Debets who will join the group after being awarded a PhD position in the NWO graduate program; Future Medicine


Congratulations to Ana for having her manuscript accepted in Journal of Proteomics


Congratulations to Thierry for having his manuscript accepted in Proteomics



Diet-Induced Neuropeptide Expression: Feasibility of Quantifying Extended and Highly Charged Endogenous Peptide Sequences by Selected Reaction Monitoring

Understanding regulation and action of endogenous peptides, especially neuropeptides, which serve as inter- and intracellular signal transmitters, is key in understanding a variety of functional processes, such as energy balance, memory, circadian rhythm, drug addiction, etc. Therefore, accurate and reproducible quantification of these bioactive endogenous compounds is highly relevant. The

PhosphoPath: Visualization of Phosphosite-centric Dynamics in Temporal Molecular Networks

Protein phosphorylation is an essential post-translational modification (PTM) regulating many biological processes at the cellular and multicellular level. Continuous improvements in phosphoproteomics technology allow the analysis of this PTM in an expanding biological content. Yet, up till now proteome data visualization tools are still very gene centric, hampering the ability

Signal Transduction Reaction Monitoring Deciphers Site-Specific PI3K-mTOR/MAPK Pathway Dynamics in Oncogene-Induced Senescence

We report a straightforward strategy to comprehensively monitor signal transduction pathway dynamics in mammalian systems. Combining targeted quantitative proteomics with highly selective phosphopeptide enrichment, we monitor, with great sensitivity, phosphorylation dynamics of the PI3K-mTOR and MAPK signaling networks. Our approach consists of a single enrichment step followed by a single

Benchmarking multiple fragmentation methods on an orbitrap fusion for top-down phospho-proteoform characterization.

Top-down analysis of intact proteins by mass spectrometry provides an ideal platform for comprehensive proteoform characterization, in particular, for the identification and localization of post-translational modifications (PTM) co-occurring on a protein. One of the main bottlenecks in top-down proteomics is insufficient protein sequence coverage caused by incomplete protein fragmentation. Based

ROCK1 is a potential combinatorial drug target for BRAF mutant melanoma

Treatment of BRAF mutant melanomas with specific BRAF inhibitors leads to tumor remission. However, most patients eventually relapse due to drug resistance. Therefore, we designed an integrated strategy using (phospho)proteomic and functional genomic platforms to identify drug targets whose inhibition sensitizes melanoma cells to BRAF inhibition. We found many proteins

Single-step enrichment by Ti4+-IMAC and label-free quantitation enables in-depth monitoring of phosphorylation dynamics with high reproducibility and temporal resolution.

Quantitative phosphoproteomics workflows traditionally involve additional sample labeling and fractionation steps for accurate and in-depth analysis. Here we report a high-throughput, straightforward, and comprehensive label-free phosphoproteomics approach using the highly selective, reproducible, and sensitive Ti(4+)-IMAC phosphopeptide enrichment method. We demonstrate the applicability of this approach by monitoring the phosphoproteome dynamics