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N-terminal domain mutations and their effects on prion protein copper binding, octapeptide repeat expansion, and aggregation propensity are diagrammed.

Figure 4

Diagram

Source Paper

Mutations in Prion Protein Gene: Pathogenic Mechanisms in C-Terminal vs. N-Terminal Domain, a Review.

International journal of molecular sciences (2019)

PMID: 31340582

DOI: 10.3390/ijms20143606

Cite This Figure

![Figure 4: N-terminal domain mutations and their effects on prion protein copper binding, octapeptide repeat expansion, and aggregation propensity are diagrammed.]()

> 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/)
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  <img src="" alt="N-terminal domain mutations and their effects on prion protein copper binding, octapeptide repeat expansion, and aggregation propensity are diagrammed." />
  <figcaption>Figure 4. N-terminal domain mutations and their effects on prion protein copper binding, octapeptide repeat expansion, and aggregation propensity are diagrammed.<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>
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