Discriminating taste of prions
Article Abstract:
The mechanisms underlying the conversion of yeast prion proteins to an infectious form are clarified. Researchers have used an array assay for analyzing the ability of the amino-acid sequences to bind and to modify the full-length protein and have concluded that the small elements of the Sup35 amino-acid sequence can recognize soluble conformations of the protein with unusual specificity, which is sufficient for converting the soluble proteins to the abnormal prion state.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 2007
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Prions and their partners in crime
Article Abstract:
Prions, the infectious agents of transmissible spongiform encephalopathies (TSEs), lack nucleic acids and are composed of a pathological, self-inducing form of the host's prion protein (PrP). Interactions between TSE-associated PrP and its normal counterpart are also pathologically important, so the physiological functions of normal PrP and how they might be corrupted by TSE infections are investigated.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 2006
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Designer prions
Article Abstract:
The design of prion based on the aggregation properties of tracts of glutamine amino acids is discussed. The asparagine or glutamine rich region is essential for aggregation.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 2004
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