Prions are affected by evolution at two levels

Cellular and Molecular Life Sciences

Volumn 73, Issue 6, 2016, Pages 1131-1144

  Wickner, Reed B ^a   Kelly, Amy C ^a,b  

^a NATIONAL INSTITUTES OF HEALTH   (United States)

^b AGRICULTURAL RESEARCH SERVICE   (United States)

Author keywords

Amyloid; HET s; Parallel in register beta sheet; Rnq1; Sup35p; Ure2p

Indexed keywords

HET S PROTEIN; PLASMID DNA; PRION PROTEIN; RNQ1P PROTEIN; SUP35P PROTEIN; UNCLASSIFIED DRUG; URE2P PROTEIN; AMYLOID; FUNGAL PROTEIN; GLUTATHIONE PEROXIDASE; HET-S PROTEIN, PODOSPORA ANSERINA; PRION; SACCHAROMYCES CEREVISIAE PROTEIN; SUP35 PROTEIN, S CEREVISIAE; TRANSLATION TERMINATION FACTOR; URE2 PROTEIN, S CEREVISIAE;

AMINO TERMINAL SEQUENCE; BETA SHEET; BOVINE SPONGIFORM ENCEPHALOPATHY; CARBOXY TERMINAL SEQUENCE; CHRONIC WASTING DISEASE; CREUTZFELDT JAKOB DISEASE; EVOLUTION; FELINE SPONGIFORM ENCEPHALOPATHY; GENETIC VARIABILITY; HUMAN; INCIDENCE; MAMMAL; NONHUMAN; PODOSPORA ANSERINA; PROTEIN CONFORMATION; PROTEIN POLYMORPHISM; REVIEW; SCRAPIE; YEAST; ANALYSIS; ANIMAL; CHEMISTRY; GENETICS; METABOLISM; MOLECULAR EVOLUTION; PATHOLOGY; PODOSPORA; PRION; PRION DISEASE; SACCHAROMYCES CEREVISIAE;

AMYLOID; ANIMALS; EVOLUTION, MOLECULAR; FUNGAL PROTEINS; GLUTATHIONE PEROXIDASE; HUMANS; PEPTIDE TERMINATION FACTORS; PODOSPORA; PRION DISEASES; PRIONS; PROTEIN CONFORMATION; SACCHAROMYCES CEREVISIAE; SACCHAROMYCES CEREVISIAE PROTEINS;

EID: 84958742200     PISSN: 1420682X     EISSN: 14209071     Source Type: Journal    
DOI: 10.1007/s00018-015-2109-6     Document Type: Review

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