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@ARTICLE{Heise:276,
      author       = {Heise, H. and Celej, M.S. and Becker, S. and Riedel, D. and
                      Pelah, A. and Kumar, A. and Jovin, T.M. and Baldus, M.},
      title        = {{S}olid-state {NMR} reveals structural differences between
                      fibrils of wild-type and disease-related {A}53{T} mutant
                      alpha-synuclein},
      journal      = {Journal of molecular biology},
      volume       = {380},
      issn         = {0022-2836},
      address      = {Amsterdam [u.a.]},
      publisher    = {Elsevier},
      reportid     = {PreJuSER-276},
      pages        = {444 - 450},
      year         = {2008},
      note         = {Record converted from VDB: 12.11.2012},
      abstract     = {Fibrils from the Parkinson's-disease-related A53T mutant of
                      alpha-synuclein were investigated by solid-state NMR
                      spectroscopy, electron microscopy, and atomic force
                      microscopy. Sequential solid-state NMR resonance assignments
                      were obtained for a large fraction of the fibril core.
                      Experiments conducted above and below the freezing point
                      suggest that the fibrils contain regions with increased
                      mobility and structural elements different from beta-strand
                      character, in addition to the rigid beta-sheet-rich core
                      region. As in earlier studies on wild-type alpha-synuclein,
                      the C-terminus was found to be flexible and unfolded,
                      whereas the main core region was highly rigid and rich in
                      beta-sheets. Compared to fibrils from wild-type
                      alpha-synuclein, the well-ordered beta-sheet region extends
                      to at least L38 and L100. These results demonstrate that a
                      disease-related mutant of alpha-synuclein differs in both
                      aggregation kinetics and fibril structure.},
      keywords     = {Amino Acid Sequence / Escherichia coli: genetics / Freezing
                      / Humans / Microscopy, Atomic Force / Microscopy, Electron /
                      Molecular Sequence Data / Mutation / Nuclear Magnetic
                      Resonance, Biomolecular: methods / Parkinson Disease:
                      genetics / Parkinson Disease: pathology / Protein Structure,
                      Secondary / Recombinant Proteins: chemistry / Recombinant
                      Proteins: metabolism / Recombinant Proteins: ultrastructure
                      / alpha-Synuclein: chemistry / alpha-Synuclein: genetics /
                      alpha-Synuclein: metabolism / alpha-Synuclein:
                      ultrastructure / Recombinant Proteins (NLM Chemicals) /
                      alpha-Synuclein (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    = {Biochemistry $\&$ Molecular Biology},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:18539297},
      UT           = {WOS:000257564000002},
      doi          = {10.1016/j.jmb.2008.05.026},
      url          = {https://juser.fz-juelich.de/record/276},
}