Beschreibung
Structural comparison between normal cellular PrPC and misfolded PrPSc conformations highlights the beta-sheet enrichment that characterizes the pathogenic isoform.
Figure 5
DiagramSource Paper
Mutations in Prion Protein Gene: Pathogenic Mechanisms in C-Terminal vs. N-Terminal Domain, a Review.Cite This Figure
![Figure 5: Structural comparison between normal cellular PrPC and misfolded PrPSc conformations highlights the beta-sheet enrichment that characterizes the pathogenic isoform.]() > Source: Livia Bernardi et al. "Mutations in Prion Protein Gene: Pathogenic Mechanisms in C-Terminal vs. N-Termi." *International journal of molecular sciences*, 2019. PMID: [31340582](https://pubmed.ncbi.nlm.nih.gov/31340582/)
<figure> <img src="" alt="Structural comparison between normal cellular PrPC and misfolded PrPSc conformations highlights the beta-sheet enrichment that characterizes the pathogenic isoform." /> <figcaption>Figure 5. Structural comparison between normal cellular PrPC and misfolded PrPSc conformations highlights the beta-sheet enrichment that characterizes the pathogenic isoform.<br> Source: Livia Bernardi et al. "Mutations in Prion Protein Gene: Pathogenic Mechanisms in C-Terminal vs. N-Termi." <em>International journal of molecular sciences</em>, 2019. PMID: <a href="https://pubmed.ncbi.nlm.nih.gov/31340582/">31340582</a></figcaption> </figure>