Solid-State Nuclear Magnetic Resonance on the Static and Dynamic Domains of Huntingtin Exon-1 Fibrils.

@article{Isas2015SolidStateNM,
  title={Solid-State Nuclear Magnetic Resonance on the Static and Dynamic Domains of Huntingtin Exon-1 Fibrils.},
  author={Jose Mario Isas and Ralf Langen and Ansgar B Siemer},
  journal={Biochemistry},
  year={2015},
  volume={54 25},
  pages={3942-9}
}
Amyloid-like fibrils formed by huntingtin exon-1 (htt_ex1) are a hallmark of Huntington's disease (HD). The structure of these fibrils is unknown, and determining their structure is an important step toward understanding the misfolding processes that cause HD. In HD, a polyglutamine (polyQ) domain in htt_ex1 is expanded to a degree that it gains the ability to form aggregates comprising the core of the resulting fibrils. Despite the simplicity of this polyQ sequence, the structure of htt_ex1… CONTINUE READING
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Fibrils Determined by Solid-State Nuclear Magnetic Resonance

  • M. Michalek, E. S. Salnikov, S. Werten, B. Bechinger
  • Biochemistry 52,
  • 2013

proline) form II in the crystalline state as studied by high-resolution solid-state 13C NMR spectroscopy

  • R. Graf, H. W. Spiess, +4 authors H. Iatrou
  • J. Mol. Struct. 317,
  • 2012

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