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@ARTICLE{Esch:166795,
      author       = {Esch, Daniel and Vahokoski, Juha and Groves, Matthew and
                      Pogenberg, Vivian and Cojocaru, Vlad and vom Bruch, Hermann
                      and Han, Dong and Drexler, Hannes C. A. and Araúzo-Bravo,
                      Marcos J. and Ng, Calista K. L. and Jauch, Ralf and
                      Wilmanns, Matthias and Schöler, Hans R.},
      title        = {{A} unique {O}ct4 interface is crucial for reprogramming to
                      pluripotency},
      journal      = {Nature cell biology},
      volume       = {15},
      number       = {3},
      issn         = {1476-4679},
      address      = {New York, NY},
      publisher    = {Nature America},
      reportid     = {DESY-2014-01629},
      pages        = {295 - 301},
      year         = {2013},
      note         = {© Macmillan Publishers Limited.; Post referee fulltext in
                      progress; Embargo 6 months from publication},
      abstract     = {Terminally differentiated cells can be reprogrammed to
                      pluripotency by the forced expression of Oct4, Sox2, Klf4
                      and c-Myc. However, it remains unknown how this leads to the
                      multitude of epigenetic changes observed during the
                      reprogramming process. Interestingly, Oct4 is the only
                      factor that cannot be replaced by other members of the same
                      family to induce pluripotency. To understand the unique role
                      of Oct4 in reprogramming, we determined the structure of its
                      POU domain bound to DNA. We show that the linker between the
                      two DNA-binding domains is structured as an α-helix and
                      exposed to the protein's surface, in contrast to the
                      unstructured linker of Oct1. Point mutations in this
                      α-helix alter or abolish the reprogramming activity of
                      Oct4, but do not affect its other fundamental properties. On
                      the basis of mass spectrometry studies of the interactome of
                      wild-type and mutant Oct4, we propose that the linker
                      functions as a protein-protein interaction interface and
                      plays a crucial role during reprogramming by recruiting key
                      epigenetic players to Oct4 target genes. Thus, we provide
                      molecular insights to explain how Oct4 contributes to the
                      reprogramming process.},
      cin          = {EMBL},
      ddc          = {570},
      cid          = {I:(DE-H253)EMBL-20120731},
      pnm          = {DORIS Beamline K1.2 (POF2-54G13) / DORIS Beamline K1.3
                      (POF2-54G13)},
      pid          = {G:(DE-H253)POF2-K1.2-20130405 /
                      G:(DE-H253)POF2-K1.3-20130405},
      experiment   = {EXP:(DE-H253)D-K1.2-20150101 /
                      EXP:(DE-H253)D-K1.3-20150101},
      typ          = {PUB:(DE-HGF)16},
      UT           = {WOS:000315844900010},
      pubmed       = {pmid:23376973},
      doi          = {10.1038/ncb2680},
      url          = {https://bib-pubdb1.desy.de/record/166795},
}