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@ARTICLE{Wrdehoff:203194,
      author       = {Wördehoff, Michael M. and Bannach, Oliver and
                      Shaykhalishahi, Hamed and Kulawik, Andreas and Schiefer,
                      Stephanie and Willbold, Dieter and Hoyer, Wolfgang and
                      Birkmann, Eva},
      title        = {{S}ingle {F}ibril {G}rowth {K}inetics of α-{S}ynuclein},
      journal      = {Journal of molecular biology},
      volume       = {427},
      number       = {6 B},
      issn         = {0022-2836},
      address      = {Amsterdam [u.a.]},
      publisher    = {Elsevier},
      reportid     = {FZJ-2015-05195},
      pages        = {1428 - 1435},
      year         = {2015},
      abstract     = {Neurodegenerative disorders associated with protein
                      misfolding are fatal diseases that are caused by
                      fibrillation of endogenous proteins such as α-synuclein
                      (α-syn) in Parkinson's disease (PD) or amyloid-β in
                      Alzheimer's disease. Fibrils of α-syn are a major
                      pathological hallmark of PD and certain aggregation
                      intermediates are postulated to cause synaptic failure and
                      cell death of dopaminergic neurons in the substantia nigra.
                      For the development of therapeutic approaches, the
                      mechanistic understanding of the fibrillation process is
                      essential. Here we report real-time observation of α-syn
                      fibril elongation on a glass surface, imaged by total
                      internal reflection fluorescence microscopy using thioflavin
                      T fluorescence. Fibrillation on the glass surface occurred
                      in the same time frame and yielded fibrils of similar length
                      as fibrillation in solution. Time-resolved imaging of
                      fibrillation on a single fibril level indicated that α-syn
                      fibril elongation follows a stop-and-go mechanism; that is,
                      fibrils either extend at a homogenous growth rate or stop to
                      grow for variable time intervals. The fibril growth kinetics
                      were compatible with a model featuring two states, a growth
                      state and a stop state, which were approximately
                      isoenergetic and interconverted with rate constants of ~ 1.5
                      × 10− 4 s− 1. In the growth state, α-syn monomers were
                      incorporated into the fibril with a rate constant of 8.6 ×
                      103 M− 1 s− 1. Fibril elongation of α-syn is slow
                      compared to other amyloidogenic proteins.},
      cin          = {ICS-6},
      ddc          = {570},
      cid          = {I:(DE-Juel1)ICS-6-20110106},
      pnm          = {553 - Physical Basis of Diseases (POF3-553)},
      pid          = {G:(DE-HGF)POF3-553},
      typ          = {PUB:(DE-HGF)16},
      UT           = {WOS:000351798700016},
      pubmed       = {pmid:25659910},
      doi          = {10.1016/j.jmb.2015.01.020},
      url          = {https://juser.fz-juelich.de/record/203194},
}