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@ARTICLE{Watson:140870,
      author       = {Watson, A. A. and Mahajan, P. and Mertens, H. D. and Deery,
                      M. J. and Zhang, W. and Pham, P. and Du, X. and Bartke, T.
                      and Edlich, C. and Berridge, G. and Chen, Y. and
                      Burgess-Brown, N. A. and Kouzarides, T. and Wiechens, N. and
                      Owen-Hughes, T. and Svergun, D. I. and Gileadi, O. and Laue,
                      E. D. and DESY},
      title        = {{T}he {PHD} and chromo domains regulate the {ATP}ase
                      activity of the human chromatin remodeler {CHD}4},
      journal      = {Journal of molecular biology},
      volume       = {422},
      issn         = {0022-2836},
      address      = {Amsterdam [u.a.]},
      publisher    = {Elsevier},
      reportid     = {PHPPUBDB-24948},
      pages        = {3-17},
      year         = {2012},
      abstract     = {The NuRD (nucleosome remodeling and deacetylase) complex
                      serves as a crucial epigenetic regulator of cell
                      differentiation, proliferation, and hematopoietic
                      development by coupling the deacetylation and demethylation
                      of histones, nucleosome mobilization, and the recruitment of
                      transcription factors. The core nucleosome remodeling
                      function of the mammalian NuRD complex is executed by the
                      helicase-domain-containing ATPase CHD4 (Mi-2β) subunit,
                      which also contains N-terminal plant homeodomain (PHD) and
                      chromo domains. The mode of regulation of chromatin
                      remodeling by CHD4 is not well understood, nor is the role
                      of its PHD and chromo domains. Here, we use small-angle
                      X-ray scattering, nucleosome binding ATPase and remodeling
                      assays, limited proteolysis, cross-linking, and tandem mass
                      spectrometry to propose a three-dimensional structural model
                      describing the overall shape and domain interactions of CHD4
                      and discuss the relevance of these for regulating the
                      remodeling of chromatin by the NuRD complex.},
      keywords     = {Adenosine Triphosphatases: metabolism / Autoantigens:
                      chemistry / Autoantigens: metabolism / Binding Sites /
                      Chromatin: metabolism / Chromatin Assembly and Disassembly /
                      Electrophoretic Mobility Shift Assay / Humans / Mi-2
                      Nucleosome Remodeling and Deacetylase Complex: chemistry /
                      Mi-2 Nucleosome Remodeling and Deacetylase Complex:
                      metabolism / Models, Biological / Nucleosomes: metabolism /
                      Protein Structure, Tertiary / Proteolysis / Autoantigens
                      (NLM Chemicals) / CHD4 protein, human (NLM Chemicals) /
                      Chromatin (NLM Chemicals) / Nucleosomes (NLM Chemicals) /
                      Mi-2 Nucleosome Remodeling and Deacetylase Complex (NLM
                      Chemicals) / Adenosine Triphosphatases (NLM Chemicals)},
      cin          = {EMBL},
      ddc          = {570},
      cid          = {$I:(DE-H253)EMBL_-2012_-20130307$},
      pnm          = {DORIS Beamline D1.2 (POF2-54G13)},
      pid          = {G:(DE-H253)POF2-D1.2-20130405},
      experiment   = {EXP:(DE-H253)D-D1.2-20150101},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:22575888},
      pmc          = {pmc:PMC3437443},
      UT           = {WOS:000308267700002},
      doi          = {10.1016/j.jmb.2012.04.031},
      url          = {https://bib-pubdb1.desy.de/record/140870},
}