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@ARTICLE{Staal:127545,
      author       = {J. A. Staal and L. S. Lau and H. Zhang and W. J. Ingram and
                      A. R. Hallahan and P. A. Northcott$^*$ and S. Pfister$^*$
                      and R. J. Wechsler-Reya and J. M. Rusert and M. D. Taylor
                      and Y.-J. Cho and R. J. Packer and K. J. Brown and B. R.
                      Rood},
      title        = {{P}roteomic profiling of high risk medulloblastoma reveals
                      functional biology.},
      journal      = {OncoTarget},
      volume       = {6},
      number       = {16},
      issn         = {1949-2553},
      address      = {[S.l.]},
      publisher    = {Impact Journals LLC},
      reportid     = {DKFZ-2017-03568},
      pages        = {14584 - 14595},
      year         = {2015},
      abstract     = {Genomic characterization of medulloblastoma has improved
                      molecular risk classification but struggles to define
                      functional biological processes, particularly for the most
                      aggressive subgroups. We present here a novel proteomic
                      approach to this problem using a reference library of stable
                      isotope labeled medulloblastoma-specific proteins as a
                      spike-in standard for accurate quantification of the tumor
                      proteome. Utilizing high-resolution mass spectrometry, we
                      quantified the tumor proteome of group 3 medulloblastoma
                      cells and demonstrate that high-risk MYC amplified tumors
                      can be segregated based on protein expression patterns. We
                      cross-validated the differentially expressed protein
                      candidates using an independent transcriptomic data set and
                      further confirmed them in a separate cohort of
                      medulloblastoma tissue samples to identify the most robust
                      proteogenomic differences. Interestingly, highly expressed
                      proteins associated with MYC-amplified tumors were
                      significantly related to glycolytic metabolic pathways via
                      alternative splicing of pyruvate kinase (PKM) by
                      heterogeneous ribonucleoproteins (HNRNPs). Furthermore, when
                      maintained under hypoxic conditions, these MYC-amplified
                      tumors demonstrated increased viability compared to
                      non-amplified tumors within the same subgroup. Taken
                      together, these findings highlight the power of proteomics
                      as an integrative platform to help prioritize genetic and
                      molecular drivers of cancer biology and behavior.},
      keywords     = {Biomarkers, Tumor (NLM Chemicals)},
      cin          = {B062},
      ddc          = {610},
      cid          = {I:(DE-He78)B062-20160331},
      pnm          = {312 - Functional and structural genomics (POF3-312)},
      pid          = {G:(DE-HGF)POF3-312},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:25970789},
      pmc          = {pmc:PMC4546489},
      doi          = {10.18632/oncotarget.3927},
      url          = {https://inrepo02.dkfz.de/record/127545},
}