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@ARTICLE{Simon:856430,
      author       = {Simon, Paul and Grüner, Daniel and Worch, Hartmut and
                      Pompe, Wolfgang and Lichte, Hannes and El Khassawna, Thaqif
                      and Heiss, Christian and Wenisch, Sabine and Kniep,
                      Rüdiger},
      title        = {{F}irst {E}vidence of {O}ctacalcium
                      {P}hosphate@{O}steocalcin {N}anocomplex as {S}keletal {B}one
                      {C}omponent {D}irecting {C}ollagen {T}riple–{H}elix
                      {N}anofibril {M}ineralization},
      journal      = {Scientific reports},
      volume       = {8},
      number       = {1},
      issn         = {2045-2322},
      address      = {[London]},
      publisher    = {Macmillan Publishers Limited, part of Springer Nature},
      reportid     = {FZJ-2018-05829},
      pages        = {13696},
      year         = {2018},
      abstract     = {Tibia trabeculae and vertebrae of rats as well as human
                      femur were investigated by high-resolution TEM at the atomic
                      scale in order to reveal snapshots of the morphogenetic
                      processes of local bone ultrastructure formation. By taking
                      into account reflections of hydroxyapatite for Fourier
                      filtering the appearance of individual alpha–chains within
                      the triple–helix clearly shows that bone bears the feature
                      of an intergrowth composite structure extending from the
                      atomic to the nanoscale, thus representing a molecular
                      composite of collagen and apatite. Careful Fourier analysis
                      reveals that the non–collagenous protein osteocalcin is
                      present directly combined with octacalcium phosphate.
                      Besides single spherical specimen of about 2 nm in
                      diameter, osteocalcin is spread between and over collagen
                      fibrils and is often observed as pearl necklace strings. In
                      high-resolution TEM, the three binding sites of the
                      γ-carboxylated glutamic acid groups of the mineralized
                      osteocalcin were successfully imaged, which provide the
                      chemical binding to octacalcium phosphate. Osteocalcin is
                      attached to the collagen structure and interacts with the
                      Ca–sites on the (100) dominated hydroxyapatite platelets
                      with Ca-Ca distances of about 9.5 Å. Thus, osteocalcin
                      takes on the functions of Ca–ion transport and suppression
                      of hydroxyapatite expansion.},
      cin          = {IEK-2},
      ddc          = {600},
      cid          = {I:(DE-Juel1)IEK-2-20101013},
      pnm          = {111 - Efficient and Flexible Power Plants (POF3-111)},
      pid          = {G:(DE-HGF)POF3-111},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:30209287},
      UT           = {WOS:000444377500016},
      doi          = {10.1038/s41598-018-31983-5},
      url          = {https://juser.fz-juelich.de/record/856430},
}