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@ARTICLE{Chrabszczewska:461912,
      author       = {Chrabąszczewska, Magdalena and Sieradzan, Adam K. and
                      Rodziewicz-Motowidło, Sylwia and Grubb, Anders and Dobson,
                      Christopher M. and Kumita, Janet R. and Kozak, Maciej},
      title        = {{S}tructural {C}haracterization of {C}ovalently
                      {S}tabilized {H}uman {C}ystatin {C} {O}ligomers},
      journal      = {International journal of molecular sciences},
      volume       = {21},
      number       = {16},
      issn         = {1422-0067},
      address      = {Basel},
      publisher    = {Molecular Diversity Preservation International},
      reportid     = {PUBDB-2021-03169},
      pages        = {5860},
      year         = {2020},
      abstract     = {Human cystatin C (HCC), a cysteine-protease inhibitor,
                      exists as a folded monomer under physiological conditions
                      but has the ability to self-assemble via domain swapping
                      into multimeric states, including oligomers with a
                      doughnut-like structure. The structure of the monomeric HCC
                      has been solved by X-ray crystallography, and a covalently
                      linked version of HCC (stab-1 HCC) is able to form stable
                      oligomeric species containing 10–12 monomeric subunits. We
                      have performed molecular modeling, and in conjunction with
                      experimental parameters obtained from atomic force
                      microscopy (AFM), transmission electron microscopy (TEM) and
                      small-angle X-ray scattering (SAXS) measurements, we observe
                      that the structures are essentially flat, with a height of
                      about 2 nm, and the distance between the outer edge of the
                      ring and the edge of the central cavity is ~5.1 nm. These
                      dimensions correspond to the height and diameter of one
                      stab-1 HCC subunit and we present a dodecamer model for
                      stabilized cystatin C oligomers using molecular dynamics
                      simulations and experimentally measured parameters. Given
                      that oligomeric species in protein aggregation reactions are
                      often transient and very highly heterogeneous, the
                      structural information presented here on these isolated
                      stab-1 HCC oligomers may be useful to further explore the
                      physiological relevance of different structural species of
                      cystatin C in relation to protein misfolding disease.},
      cin          = {EMBL-User / FS-PS},
      ddc          = {540},
      cid          = {I:(DE-H253)EMBL-User-20120814 / I:(DE-H253)FS-PS-20131107},
      pnm          = {899 - ohne Topic (POF4-899)},
      pid          = {G:(DE-HGF)POF4-899},
      experiment   = {EXP:(DE-H253)D-D1.2-20150101},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {32824145},
      UT           = {WOS:000565053900001},
      doi          = {10.3390/ijms21165860},
      url          = {https://bib-pubdb1.desy.de/record/461912},
}