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@ARTICLE{Leliveld:59552,
      author       = {Leliveld, S. R. and Korth, C.},
      title        = {{T}he use of conformation-specific ligands and assays to
                      dissect the molecular mechanisms of neurodegenerative
                      diseases},
      journal      = {Journal of neuroscience research},
      volume       = {85},
      issn         = {0360-4012},
      address      = {New York, NY [u.a.]},
      publisher    = {Wiley-Liss},
      reportid     = {PreJuSER-59552},
      pages        = {2285 - 2297},
      year         = {2007},
      note         = {Record converted from VDB: 12.11.2012},
      abstract     = {The use of conformation-specific ligands has been closely
                      linked to progress in the molecular characterization of
                      neurodegenerative diseases. Deposition of misfolded or
                      misprocessed proteins is now recognized as a hallmark of all
                      neurodegenerative diseases. Initially, dyes like Congo red
                      and thioflavin T were used as crudely conformation-specific
                      ligands for staining the beta-sheeted protein components of
                      amyloid deposits in neurodegenerative diseases such as
                      Alzheimer disease (AD) and prion disease, the two diseases
                      in which protein conformations were distinguished early on.
                      This conformational characterization of extracellular
                      protein deposits with dyes ultimately led to the
                      identification of key players in the disease processes. The
                      recent discovery of intermediate conformational species,
                      i.e., soluble oligomers for AD and PK-sensitive PrP(Sc) for
                      prion disease, whose conformation and assembly are thought
                      to be distinct from both the physiological and the fibrillar
                      conformational states, replaced the former notion that the
                      microscopic protein deposits themselves caused disease. This
                      insight and the generation of conformation-specific
                      monoclonal antibodies to these conformers further advanced
                      diagnosis and the understanding of molecular mechanisms of
                      AD and are likely to do so in other neurodegenerative
                      diseases. Here we review how conformer distinction performed
                      by a variety of different techniques, including biophysical,
                      biochemical, and antibody-based methods, led to the current
                      molecular concepts of AD and the prion diseases. We provide
                      an outlook on the application of these techniques in
                      advancing the understanding of molecular mechanisms of other
                      neurodegenerative diseases or degenerative brain
                      conditions.},
      keywords     = {Amyloid beta-Peptides: chemistry / Animals / Antibodies,
                      Monoclonal / Brain: pathology / Brain Chemistry / Humans /
                      Ligands / Neurodegenerative Diseases: diagnosis /
                      Neurodegenerative Diseases: pathology / Peptides: chemistry
                      / PrPSc Proteins: chemistry / Protein Conformation / Amyloid
                      beta-Peptides (NLM Chemicals) / Antibodies, Monoclonal (NLM
                      Chemicals) / Ligands (NLM Chemicals) / Peptides (NLM
                      Chemicals) / PrPSc Proteins (NLM Chemicals) / J (WoSType)},
      cin          = {INB-2},
      ddc          = {570},
      cid          = {I:(DE-Juel1)VDB805},
      pnm          = {Funktion und Dysfunktion des Nervensystems},
      pid          = {G:(DE-Juel1)FUEK409},
      shelfmark    = {Neurosciences},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:17497676},
      UT           = {WOS:000248971500001},
      doi          = {10.1002/jnr.21353},
      url          = {https://juser.fz-juelich.de/record/59552},
}