NMR structure of the human prion protein with the pathological Q212P mutation reveals unique structural features

Keyphrases

• Structural Features 100%
• Prion Protein 100%
• Prion Disease 100%
• NMR Structure 100%
• PrPSc 100%
• PrPC 66%
• Structural Difference 33%
• Brain Regions 33%
• Early Events 33%
• Helix 33%
• Secondary Structure 33%
• Upstream Open Reading Frame (uORF) 33%
• Terminal End 33%
• Misfolding 33%
• Glutamine 33%
• Neuronal Cell Death 33%
• Recombinant Human 33%
• Conformational Transition 33%
• NMR Solution Structure 33%
• Proline 33%
• Disease-causing mutations 33%
• Loop Region 33%
• Prion 33%
• Hydrophobic Core 33%
• Familial Cases 33%
• Spontaneous Generation 33%
• Cellular Prion Protein 33%
• Scrapie 33%
• Neuronal Cell Degeneration 33%
• PrP Structure 33%
• Spontaneous Formation 33%
• Gene PRNP 33%
• PrP Gene 33%
• Gerstmann 33%
• Neurodegenerative Disorders 33%
• Disordered Tail 33%
• Globular Domains 33%

Biochemistry, Genetics and Molecular Biology

• Prion Protein 100%
• Wild Type 20%
• Cell Death 20%
• Conformational Change 20%
• Isoform 20%
• C-Terminus 20%
• Protein Secondary Structure 20%
• Open Reading Frame 20%
• Glutamine 20%
• Cell Degeneration 20%
• Transmissible Spongiform Encephalopathy 20%
• Scrapie 20%
• Proline 20%
• Solution Structure 20%
• PRNP 20%