% IMPORTANT: The following is UTF-8 encoded.  This means that in the presence
% of non-ASCII characters, it will not work with BibTeX 0.99 or older.
% Instead, you should use an up-to-date BibTeX implementation like “bibtex8” or
% “biber”.

@ARTICLE{Wrdehoff:838456,
      author       = {Wördehoff, MM and Shaykhalishahi, Hamed and Groß, L. and
                      Gremer, Lothar and Stoldt, Matthias and Buell, AK and
                      Willbold, Dieter and Hoyer, Wolfgang},
      title        = {{O}pposed effects of dityrosine formation in soluble and
                      aggregated alpha-synuclein on fibril growth},
      journal      = {Journal of molecular biology},
      volume       = {429},
      issn         = {0022-2836},
      address      = {Amsterdam [u.a.]},
      publisher    = {Elsevier},
      reportid     = {FZJ-2017-07059},
      pages        = {3018-3030},
      year         = {2017},
      abstract     = {Parkinson's disease is the second most common
                      neurodegenerative disease. It is characterized by
                      aggregation of the protein α-synuclein (α-syn) in Lewy
                      bodies, mitochondrial dysfunction, and increased oxidative
                      stress in the substantia nigra. Oxidative stress leads to
                      several modifications of biomolecules including dityrosine
                      (DiY) crosslinking in proteins, which has recently been
                      detected in α-syn in Lewy bodies from Parkinson's disease
                      patients. Here we report that α-syn is highly susceptible
                      to ultraviolet-induced DiY formation. We investigated DiY
                      formation of α-syn and nine tyrosine-to-alanine mutants and
                      monitored its effect on α-syn fibril formation in vitro.
                      Ultraviolet irradiation of intrinsically disordered α-syn
                      generates DiY-modified monomers and dimers, which inhibit
                      fibril formation of unmodified α-syn by interfering with
                      fibril elongation. The inhibition depends on both the DiY
                      group and its integration into α-syn. When preformed α-syn
                      fibrils are crosslinked by DiY formation, they gain
                      increased resistance to denaturation. DiY-stabilized α-syn
                      fibrils retain their high seeding efficiency even after
                      being exposed to denaturant concentrations that completely
                      depolymerize non-crosslinked seeds. Oxidative
                      stress-associated DiY crosslinking of α-syn therefore
                      entails two opposing effects: (i) inhibition of aggregation
                      by DiY-modified monomers and dimers, and (ii) stabilization
                      of fibrillar aggregates against potential degradation
                      mechanisms, which can lead to promotion of aggregation,
                      especially in the presence of secondary nucleation.},
      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},
      pubmed       = {pmid:28918091},
      UT           = {WOS:000413614100004},
      doi          = {10.1016/j.jmb.2017.09.005},
      url          = {https://juser.fz-juelich.de/record/838456},
}