Spontaneous conformational change within the prion protein - Implications for disease pathogenesis?

BioEssays

Volumn 23, Issue 9, 2001, Pages 772-774

  Jackson, Graham S ^a  

^a IMPERIAL COLLEGE SCHOOL OF MEDICINE   (United Kingdom)

Author keywords

[No Author keywords available]

Indexed keywords

PRION PROTEIN; RECOMBINANT PROTEIN;

ANIMAL; CHEMISTRY; PATHOGENICITY; PATHOPHYSIOLOGY; PRION; PRION DISEASE; PROTEIN CONFORMATION; PROTEIN SECONDARY STRUCTURE; SCRAPIE; SHORT SURVEY;

ANIMALS; PRION DISEASES; PRIONS; PROTEIN CONFORMATION; PROTEIN STRUCTURE, SECONDARY; PRPC PROTEINS; PRPSC PROTEINS; RECOMBINANT PROTEINS; SCRAPIE;

EID: 0034814161     PISSN: 02659247     EISSN: None     Source Type: Journal    
DOI: 10.1002/bies.1112     Document Type: Short Survey

References (11)

1. Immobilized prion protein undergoes spontaneous rearrangement to a conformation having features in common with the infectious form
2. Conversion of α-helices into β-sheets features in the formation of the scrapie prion proteins
3. Identification of a protein that purifies with the scrapie prion
4. Structural studies of the scrapie prion protein using mass spectrometry and amino acid sequencing
5. A protease-resistant protein is a structural component of the scrapie prion
6. Novel proteinaceous infectious particles cause scrapie
7. Strain-specific prion-protein conformation determined by metal ions
8. A conformational transition at the N terminus of the prion protein features in formation of the scrapie isoform
9. Sc molecules with different conformations
10. Location and properties of metal-binding sites on the human prion protein
11. Selective oxidation of methionine residues in prion proteins