Related ArticlesUnderstanding the Effect of Disease-Related Mutations on Human Prion Protein Structure: Insights From NMR Spectroscopy.
Prog Mol Biol Transl Sci. 2017;150:83-103
Authors: Biljan I, Ilc G, Plavec J
Abstract
Prion diseases or transmissible spongiform encephalopathies constitute a group of fatal neurodegenerative diseases that can be of sporadic, genetic, or acquired origin. The central molecular event of prion diseases is the conformational conversion of the physiological cellular prion protein, PrP(C), into a disease-associated form known as prion or PrP(Sc). Spontaneous generation of prions in genetic prion diseases is caused by mutations in the human prion protein gene (PRNP). Understanding of the earliest conformational changes during misfolding of PrP(C) in genetic forms of prion diseases may benefit from detailed structural characterization of various human (Hu) PrP variants. Nuclear magnetic resonance (NMR) spectroscopy offers unique opportunities to obtain detailed atomic-level structure information. In this chapter we present an overview of high-resolution NMR studies on several HuPrPs with disease-associated mutations at mildly acidic and physiological pH conditions that provided valuable insights into possible key structural determinants underlying the formation of prions.
Prion proteins responsible for Mad cow disease, Creutzfeld-Jakob disease - News-Medical.net
Prion proteins responsible for Mad cow disease, Creutzfeld-Jakob disease - News-Medical.net
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Prion proteins responsible for Mad cow disease, Creutzfeld-Jakob disease
News-Medical.net
Kai Schlepckow and Harald Schwalbe at the Goethe University Frankfurt am Main have successfully used time-resolved NMR spectroscopic studies to follow what is happening to every individual amino acid as the prion protein molecules aggregateâ??an ...
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[NMR paper] Structural analysis of the pyroglutamate-modified isoform of the Alzheimer's disease-related amyloid-? using NMR spectroscopy.
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Toward the Molecular Basis of Inherited Prion Diseases: NMR Structure of the Human Prion Protein with V210I Mutation.
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J Mol Biol. 2011 Aug 4;
Authors: Biljan I, Ilc G, Giachin G, Raspadori A, Zhukov I, Plavec J, Legname G
The development of transmissible spongiform encephalopathies (TSEs) is associated with the conversion of the cellular prion protein (PrP(C)) into a misfolded, pathogenic isoform (PrP(Sc)). Spontaneous generation...
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08-16-2011 01:19 PM
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[NMR paper] Influence of pH on NMR structure and stability of the human prion protein globular do
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The NMR structure of the globular domain of the human prion protein (hPrP) with residues 121-230 at pH 7.0 shows the same global fold as the previously published structure determined at pH 4.5. It contains three alpha-helices, comprising residues 144-156, 174-194, and 200-228, and...
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[NMR paper] Prion protein NMR structure and familial human spongiform encephalopathies.
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The refined NMR structure of the mouse prion protein domain mPrP(121-231) and the recently reported NMR structure of the complete 208-residue polypeptide chain of mPrP are used to investigate the structural basis of inherited human transmissible...
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Understanding the Effect of Disease-Related Mutations on Human Prion Protein Structure: Insights From NMR Spectroscopy.
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