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@ARTICLE{Kastenholz:56233,
      author       = {Kastenholz, B.},
      title        = {{N}ew hope for the diagnosis and therapy of {A}lzheimer's
                      disease},
      journal      = {Protein and peptide letters},
      volume       = {14},
      issn         = {0929-8665},
      address      = {Schiphol},
      publisher    = {Bentham Science Publ.},
      reportid     = {PreJuSER-56233},
      pages        = {389 - 393},
      year         = {2007},
      note         = {Record converted from VDB: 12.11.2012},
      abstract     = {Improperly folded metal cofactor-containing proteins (e.g.,
                      copper chaperone for Superoxide dismutase, CCS) are believed
                      to play a key role in several protein-misfolding diseases
                      (e.g., Alzheimer's disease or Amyotrophic Lateral Sclerosis)
                      because Under regular physiological conditions,
                      metallochaperolles activate or stabilize the native
                      conformation of important metalloproteins (e.g., superoxide
                      dismutase) in certain Cellular processes. For an improved
                      diagnosis and therapy of neurodegenerative diseases, new
                      methodologies have to be developed that enable a
                      well-defined differentiation between properly folded and
                      inactive metalloproteins in clinical samples. In the
                      literature it is reported that different high molecular mass
                      metal-containing proteins were isolated in brain samples
                      from Alzheimer's patients and in vegetables by using a
                      2-dimensional polyacrylamide gel electrophoresis (2-DE)
                      procedure. In the present article, selected results of these
                      studies are Scrutinized and compared with some results
                      obtained by a standardized method termed 'quantitative
                      preparative native continuous polycrylamide gel
                      electrophoresis (QPNC-PAGE)'. Conclusively, QPNC-PAGE is a
                      highly efficient approach used by biochemists to resolve
                      native and denatured metalloproteins (MW 6 - >= 200 kDa) in
                      complex protein Mixtures.},
      keywords     = {J (WoSType)},
      cin          = {ICG-3},
      ddc          = {540},
      cid          = {I:(DE-Juel1)ICG-3-20090406},
      pnm          = {Terrestrische Umwelt},
      pid          = {G:(DE-Juel1)FUEK407},
      shelfmark    = {Biochemistry $\&$ Molecular Biology},
      typ          = {PUB:(DE-HGF)16},
      UT           = {WOS:000246346800012},
      doi          = {10.2174/092986607780363970},
      url          = {https://juser.fz-juelich.de/record/56233},
}