Mammalian prion proteins

Current Opinion in Structural Biology

Volumn 10, Issue 1, 2000, Pages 69-74

  Jackson, Graham S ^a   Clarke, Anthony R ^a,b  

^a IMPERIAL COLLEGE SCHOOL OF MEDICINE   (United Kingdom)

^b UNIVERSITY OF BRISTOL   (United Kingdom)

Author keywords

[No Author keywords available]

Indexed keywords

PRION PROTEIN;

BOVINE SPONGIFORM ENCEPHALOPATHY; CREUTZFELDT JAKOB DISEASE; DISEASE PREDISPOSITION; HAMSTER; HUMAN; MOLECULAR DYNAMICS; NONHUMAN; PRION; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN FOLDING; PROTEIN STABILITY; REVIEW; SCRAPIE AGENT;

EID: 0033951182     PISSN: 0959440X     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0959-440X(99)00051-2     Document Type: Review

References (42)

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10. C into protease-resistant and detergent-insoluble PrP molecules is not the only crucial step in prion replication. The authors speculate that an additional requirement may be the aggregation of newly formed PK-resistant PrP molecules into uniquely structured aggregates.
11. RES appears to be slower than growth in infectious titre, a phenomenon that can be explained either by a novel hypothesis concerning inoculum clearance from a newly infected brain or by the faster growth of compartments containing smaller polymers. Published kinetic data are all compatible with the presented mathematical model, so the nucleated polymerisation hypothesis cannot be ruled out on dynamic grounds.
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17. Sc is through a highly unfolded state that retains, at most, only this small nucleus of structure, rather than through a highly organised folding intermediate.
18. Sc subunits.
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32. Sc in each strain.
33. C is not sufficient for the propagation of infectivity.
34. RES formation that represents a potential source of therapeutic agents for transmissible spongiform encephalopathies.
35. RES propagation and pathogenesis in vivo.
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