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My research team strives to develop new diagnostic and therapeutic approaches to detect and treat children suffering from cancer earlier, better and with reduced impact on their life.
The fundamental question is how cancer cells are different from healthy, normal cells? If we understand this we will be able to better detect and kill cancer while leaving the rest of the body untouched.
Our research focusses on proteins, the structural and functional building blocks of a cell. To do this we combine genomics and proteomics, a technology that enables us to monitor all of the proteins in our body and detect how they are changed in childhood cancer. We then use computational approaches to further analyze and integrate our findings and to make them accessible to clinicians and fellow scientists around the world.
- translational portoemics in childhood cancer
- advancing precision medicine in childhood cancer
- proteolytic regulation of cell-cell communication
- computational and experimental approaches to better understand and classify proteoforms
- new algorithms in quantitative mass spectrometry data analysis
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- Origins and clinical relevance of proteoforms in pediatric malignancies (2019)
Expert Review of Proteomics, 16 (3), 185--200
- Sensitive Determination of Proteolytic Proteoforms in Limited Microscale Proteome Samples. (2019)
Molecular & cellular proteomics : MCP,
- Tumor Variant Identification That Accounts for the Unique Molecular Landscape of Pediatric Malignancies (2019)
JNCI Cancer Spectrum, 2 (4)
- HMMR acts in the PLK1-dependent spindle positioning pathway and supports neural development (2017)
- Active site specificity profiling of the matrix metalloproteinase family: Proteomic identification of 4300 cleavage sites by nine MMPs explored with structural and synthetic peptide cleavage analyses (2016)
Matrix Biology, 49, 37-60
- TAILS N-Terminomics and Proteomics Show Protein Degradation Dominates over Proteolytic Processing by Cathepsins in Pancreatic Tumors (2016)
Cell Reports, 16 (6), 1762-1773
- Active Site Specificity Profiling of the Matrix Metalloproteinase Family: Proteomic Identification of 4,300 Cleavage Sites by MMPs 1, 2, 3, 7, 8, 9, 12, 13, and 14. (2015)
- Proteome TopFIND 3.0 with TopFINDer and PathFINDer: database and analysis tools for the association of protein termini to pre- and post-translational events (2015)
Nucleic Acids Research, 43 (D1), D290-D297
- Annotating N Termini for the Human Proteome Project: N Termini and N alpha-Acetylation Status Differentiate Stable Cleaved Protein Species from Degradation Remnants in the Human Erythrocyte Proteome (2014)
Journal of Proteome Research, 13 (4), 2028-2044
- Characterization of LysargiNase for use in phosphoproteomics experiments, partII (2014)
- Ensembles of protein termini and specific proteolytic signatures as candidate biomarkers of disease (2014)
Proteomics Clinical Applications, 8 (5-6), 338-350
- LysargiNase and tryptic digest of MDA-MB 231 cell lysates (2014)
- LysargiNase mirrors trypsin for protein C-terminal and methylation-site identification (2014)
Nature Methods, 12 (1), 55--58
- Macrophage Matrix Metalloproteinase-12 Dampens Inflammation and Neutrophil Influx in Arthritis (2014)
Cell Reports, 9 (2), 618-632
- Network Analyses Reveal Pervasive Functional Regulation Between Proteases in the Human Protease Web (2014)
Plos Biology, 12 (5)
- Protein TAILS: when termini tell tales of proteolysis and function. (2013)
- Proteomic amino-termini profiling reveals targeting information for protein import into complex plastids. (2013)
- TopFIND 2.0-linking protein termini with proteolytic processing and modifications altering protein function (2012)
Nucleic Acids Research, 40 (D1), D351-D361
- TopFIND, a knowledgebase linking protein termini with function (2011)
Nature Methods, 8 (9), 703-704
- Towards kit-like 18F-labeling of marimastat, a noncovalent inhibitor drug for in vivo PET imaging cancer associated matrix metalloproteases (2011)
MedChemComm, 2 (10), 942-949
- Novel matrix metalloproteinase inhibitor [ 18F]marimastat- aryltrifluoroborate as a probe for in vivo positron emission tomography imaging in cancer (2010)
Cancer Research, 70 (19), 7562-7569
- ClC-7 requires Ostm1 as a β-subunit to support bone resorption and lysosomal function (2006)
Nature, 440 (7081), 220-223