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@ARTICLE{Lim:143827,
      author       = {J. Lim and J. H. Park and A. Baude$^*$ and J. Fellenberg
                      and J. Zustin and F. Haller and I. Krücken and H. G. Kang
                      and Y. J. Park and C. Plass$^*$ and A. M. Lindroth},
      title        = {{T}ranscriptome and protein interaction profiling in cancer
                      cells with mutations in histone {H}3.3.},
      journal      = {Scientific data},
      volume       = {5},
      issn         = {2052-4463},
      address      = {London},
      publisher    = {Nature Publ. Group},
      reportid     = {DKFZ-2019-01389},
      pages        = {180283},
      year         = {2018},
      abstract     = {Mutations of histone variant H3.3 are highly recurrent in
                      childhood glioblastoma and in young adults with Giant Cell
                      Tumor of the Bone (GCTB). The heterozygotic representation
                      of the mutations in the tumors, and with potential histone
                      H3 and H3.3 redundancy, suggest that the mutations are
                      gain-of-function by nature. To address common H3.3 point
                      mutations, we have generated data from GCTB patient samples
                      with H3.3 G34W substitutions and engineered human GFP-tagged
                      H3.3-mutated isogenic cell lines for high throughput data
                      comparisons. First, a total of thirty-six patient samples
                      and cell lines were used to acquire gene expression
                      transcriptome data using microarray and RNA-sequencing. The
                      expression data were validated with the orthogonal nCounter
                      assay. Second, to uncover the H3.3-GFP interaction proteomes
                      from the isogenic cell lines, immunoprecipitation of
                      unmutated wild type, K27M, G34R, and G34W substitutions were
                      performed. The RNA-sequencing data and the H3.3 interaction
                      proteome enable potentially important functional insight
                      into the tumorigenic process and should spur further
                      detailed analysis.},
      keywords     = {H3 histone family member 3A, human (NLM Chemicals) /
                      Histones (NLM Chemicals)},
      cin          = {C010},
      ddc          = {500},
      cid          = {I:(DE-He78)C010-20160331},
      pnm          = {313 - Cancer risk factors and prevention (POF3-313)},
      pid          = {G:(DE-HGF)POF3-313},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:30532024},
      pmc          = {pmc:PMC6289111},
      doi          = {10.1038/sdata.2018.283},
      url          = {https://inrepo02.dkfz.de/record/143827},
}