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@ARTICLE{Goerke:119332,
      author       = {S. Goerke$^*$ and K. S. Milde$^*$ and R. Bukowiecki and P.
                      Kunz$^*$ and K. Klika$^*$ and T. Wiglenda and A. Mogk and E.
                      E. Wanker and B. Bukau$^*$ and M. Ladd$^*$ and P.
                      Bachert$^*$ and M. Zaiss$^*$},
      title        = {{A}ggregation-induced changes in the chemical exchange
                      saturation transfer ({CEST}) signals of proteins.020},
      journal      = {NMR in biomedicine},
      volume       = {30},
      number       = {1},
      issn         = {0952-3480},
      address      = {New York, NY},
      publisher    = {Wiley},
      reportid     = {DKFZ-2017-00087},
      pages        = {e3665 -},
      year         = {2017},
      abstract     = {Chemical exchange saturation transfer (CEST) is an MRI
                      technique that allows mapping of biomolecules (small
                      metabolites, proteins) with nearly the sensitivity of
                      conventional water proton MRI. In living organisms, several
                      tissue-specific CEST effects have been observed and
                      successfully applied to diagnostic imaging. In these
                      studies, particularly the signals of proteins showed a
                      distinct correlation with pathological changes. However, as
                      CEST effects depend on various properties that determine and
                      affect the chemical exchange processes, the origins of the
                      observed signal changes remain to be understood. In this
                      study, protein aggregation was identified as an additional
                      process that is encoded in the CEST signals of proteins.
                      Investigation of distinct proteins that are involved in
                      pathological disorders, namely amyloid beta and huntingtin,
                      revealed a significant decrease of all protein CEST signals
                      upon controlled aggregation. This finding is of particular
                      interest with regard to diagnostic imaging of patients with
                      neurodegenerative diseases that involve amyloidogenesis,
                      such as Alzheimers or Huntingtons disease. To investigate
                      whether the observed CEST signal decrease also occurs in
                      heterogeneous mixtures of aggregated cellular proteins, and
                      thus prospectively in tissue, heat-shocked yeast cell
                      lysates were employed. Additionally, investigation of
                      different cell compartments verified the assignment of the
                      protein CEST signals to the soluble part of the proteome.
                      The results of in vitro experiments demonstrate that
                      aggregation affects the CEST signals of proteins. This
                      observation can enable hypotheses for CEST imaging as a
                      non-invasive diagnostic tool for monitoring pathological
                      alterations of the proteome in vivo.},
      cin          = {E020 / G404 / A250},
      ddc          = {610},
      cid          = {I:(DE-He78)E020-20160331 / I:(DE-He78)G404-20160331 /
                      I:(DE-He78)A250-20160331},
      pnm          = {315 - Imaging and radiooncology (POF3-315)},
      pid          = {G:(DE-HGF)POF3-315},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:27859838},
      doi          = {10.1002/nbm.3665},
      url          = {https://inrepo02.dkfz.de/record/119332},
}