The polybasic N-terminal region of the prion protein controls the physical properties of both the cellular and fibrillar forms of PrP

Samankaltaisia teoksia

• The α-helical C-terminal domain of full-length recombinant PrP converts to an in-register parallel β-sheet structure in PrP fibrils: Evidence from solid state NMR
  Tekijä: Tycko, Robert, et al.
  Julkaistu: (2010)
• Purification and Fibrillation of Full-Length Recombinant PrP
  Tekijä: Makarava, Natallia, et al.
  Julkaistu: (2017)
• Sialylation of Prion Protein Controls the Rate of Prion Amplification, the Cross-Species Barrier, the Ratio of PrP(Sc) Glycoform and Prion Infectivity
  Tekijä: Katorcha, Elizaveta, et al.
  Julkaistu: (2014)
• Molecular Structure of Amyloid Fibrils Controls the Relationship between Fibrillar Size and Toxicity
  Tekijä: Lee, Young Jin, et al.
  Julkaistu: (2011)
• Sialylation of prion protein controls the rate of prion amplification, the cross-species barrier, the ratio of PrPSc glycoform and prion infectivity.
  Tekijä: Elizaveta Katorcha, et al.
  Julkaistu: (2014-09-01)