The Solution Structure and Dynamics of Full-length Human Cerebral Dopamine Neurotrophic Factor and Its Neuroprotective Role against α-Synuclein Oligomers.

@article{Latg2015TheSS,
  title={The Solution Structure and Dynamics of Full-length Human Cerebral Dopamine Neurotrophic Factor and Its Neuroprotective Role against α-Synuclein Oligomers.},
  author={Cristiane Latg{\'e} and Katia Maria Dos Santos Cabral and Guilherme A P de Oliveira and Diana P. Raymundo and Julia A Freitas and Laizes Johanson and Luciana Ferreira Rom{\~a}o and Fernando L. Palhano and Torsten Herrmann and Marcius da Silva Almeida and Debora Foguel},
  journal={The Journal of biological chemistry},
  year={2015},
  volume={290 33},
  pages={20527-40}
}
Cerebral dopamine neurotrophic factor (CDNF) is a promising therapeutic agent for Parkinson disease. As such, there has been great interest in studying its mode of action, which remains unknown. The three-dimensional crystal structure of the N terminus (residues 9-107) of CDNF has been determined, but there have been no published structural studies on the full-length protein due to proteolysis of its C-terminal domain, which is considered intrinsically disordered. An improved purification… CONTINUE READING
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