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@ARTICLE{MartnezLumbreras:417641,
      author       = {Martínez-Lumbreras, Santiago and Krysztofinska, Ewelina M.
                      and Thapaliya, Arjun and Spilotros, Alessandro and
                      Matak-Vinkovic, Dijana and Salvadori, Enrico and Roboti,
                      Peristera and Nyathi, Yvonne and Muench, Janina H. and
                      Roessler, Maxie M. and Svergun, Dmitri I. and High, Stephen
                      and Isaacson, Rivka L.},
      title        = {{S}tructural complexity of the co-chaperone {SGTA}: a
                      conserved {C}-terminal region is implicated in dimerization
                      and substrate quality control},
      journal      = {BMC biology},
      volume       = {16},
      number       = {1},
      issn         = {1741-7007},
      address      = {Heidelberg},
      publisher    = {Springer},
      reportid     = {PUBDB-2018-05759},
      pages        = {76},
      year         = {2018},
      abstract     = {Protein quality control mechanisms are essential for cell
                      health and involve delivery of proteins to specific cellular
                      compartments for recycling or degradation. In particular,
                      stray hydrophobic proteins are captured in the aqueous
                      cytosol by a co-chaperone, the small glutamine-rich,
                      tetratricopeptide repeat-containing protein alpha (SGTA),
                      which facilitates the correct targeting of tail-anchored
                      membrane proteins, as well as the sorting of membrane and
                      secretory proteins that mislocalize to the cytosol and
                      endoplasmic reticulum-associated degradation. Full-length
                      SGTA has an unusual elongated dimeric structure that has,
                      until now, evaded detailed structural analysis. The
                      C-terminal region of SGTA plays a key role in binding a
                      broad range of hydrophobic substrates, yet in contrast to
                      the well-characterized N-terminal and TPR domains, there is
                      a lack of structural information on the C-terminal domain.
                      In this study, we present new insights into the conformation
                      and organization of distinct domains of SGTA and show that
                      the C-terminal domain possesses a conserved region essential
                      for substrate processing in vivo.},
      cin          = {EMBL-User / EMBL},
      ddc          = {610},
      cid          = {I:(DE-H253)EMBL-User-20120814 / I:(DE-H253)EMBL-20120731},
      pnm          = {6G3 - PETRA III (POF3-622)},
      pid          = {G:(DE-HGF)POF3-6G3},
      experiment   = {EXP:(DE-H253)P-P12-20150101},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:29996828},
      UT           = {WOS:000438423900002},
      doi          = {10.1186/s12915-018-0542-3},
      url          = {https://bib-pubdb1.desy.de/record/417641},
}