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@ARTICLE{Smaldone:317079,
      author       = {Smaldone, Giovanni and Pirone, Luciano and Pedone, Emilia
                      and Marlovits, Thomas and Vitagliano, Luigi and Ciccarelli,
                      Luciano},
      title        = {{T}he {BTB} domains of the potassium channel
                      tetramerization domain proteins prevalently assume
                      pentameric states},
      journal      = {FEBS letters},
      volume       = {590},
      number       = {11},
      issn         = {0014-5793},
      address      = {Chichester},
      publisher    = {Wiley},
      reportid     = {PUBDB-2017-00420},
      pages        = {1663 - 1671},
      year         = {2016},
      note         = {© Federation of European Biochemical Societies ; Post
                      referee fulltext in progress; Embargo 12 months from
                      publication},
      abstract     = {Potassium channel tetramerization domain-containing (KCTD)
                      proteins are involved in fundamental physio-pathological
                      processes. Here, we report an analysis of the oligomeric
                      state of the Bric-à-brack, Tram-track, Broad complex (BTB)
                      domains of seven distinct KCTDs belonging to five major
                      clades of the family evolution tree. Despite their
                      functional and sequence variability, present electron
                      microscopy data highlight the occurrence of well-defined
                      pentameric states for all domains. Our data also show that
                      these states coexist with alternative forms which include
                      open pentamers. Thermal denaturation analyses conducted
                      using KCTD1 as a model suggest that, in these proteins,
                      different domains cooperate to their overall stability.
                      Finally, negative-stain electron micrographs of
                      KCTD6$^{BTB}$ in complex with Cullin3 show the presence of
                      assemblies with a five-pointed pinwheel shape.},
      cin          = {CSSB-UKE / CSSB-UKE-TM},
      ddc          = {570},
      cid          = {I:(DE-H253)CSSB-UKE-20141216 /
                      I:(DE-H253)CSSB-UKE-TM-20210520},
      pnm          = {6215 - Soft Matter, Health and Life Sciences (POF3-621)},
      pid          = {G:(DE-HGF)POF3-6215},
      experiment   = {EXP:(DE-MLZ)NOSPEC-20140101},
      typ          = {PUB:(DE-HGF)16},
      UT           = {WOS:000377795000011},
      pubmed       = {pmid:27152988},
      doi          = {10.1002/1873-3468.12203},
      url          = {https://bib-pubdb1.desy.de/record/317079},
}