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@ARTICLE{Santur:856618,
      author       = {Santur, Karoline and Sevenich, Marc and Schwarten, Melanie
                      and Nischwitz, Volker and Willbold, Dieter and Mohrlüder,
                      Jeannine},
      title        = {{I}n {V}itro {R}econstitution of the {H}ighly {A}ctive and
                      {N}atively {F}olded {R}ecombinant {H}uman {S}uperoxide
                      {D}ismutase 1 {H}oloenzyme},
      journal      = {ChemistrySelect},
      volume       = {3},
      number       = {26},
      issn         = {2365-6549},
      address      = {Weinheim},
      publisher    = {Wiley-VCH},
      reportid     = {FZJ-2018-05985},
      pages        = {7627 - 7632},
      year         = {2018},
      abstract     = {SOD1 is an antioxidant enzyme that exists as a highly
                      stable dimer in healthy humans. Each subunit contains an
                      intramolecular disulfide bond and coordinates one zinc and
                      one copper ion. The dimer is destabilized in the absence of
                      the ions and disruption of the disulfide bond, which leads
                      to the formation of small oligomers and subsequently larger
                      insoluble aggregates. An acquired toxic function of
                      destabilized SOD1 is postulated to be associated with
                      amyotrophic lateral sclerosis (ALS), which is a
                      neurodegenerative disease characterized by peripheral and
                      central paralysis and by 3‐ to 5‐year median survival
                      after diagnosis. In this study, we present a protocol for
                      heterologous expression of human SOD1 in E. coli and total
                      reconstitution of the holoenzyme, which exhibits the highest
                      reported specific activity (four‐fold higher) of
                      recombinant hSOD1. Biophysical characterization confirms the
                      native state of this protein. The presented protocol
                      provides highly active hSOD1 that will benefit in vitro
                      investigations of this protein.},
      cin          = {ICS-6},
      ddc          = {540},
      cid          = {I:(DE-Juel1)ICS-6-20110106},
      pnm          = {552 - Engineering Cell Function (POF3-552)},
      pid          = {G:(DE-HGF)POF3-552},
      typ          = {PUB:(DE-HGF)16},
      UT           = {WOS:000438894200028},
      doi          = {10.1002/slct.201801319},
      url          = {https://juser.fz-juelich.de/record/856618},
}