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Volumn 8, Issue 11, 2001, Pages 958-962
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The role of conformational flexibility in prion propagation and maintenance for Sup35p
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Author keywords
[No Author keywords available]
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Indexed keywords
CHAPERONE;
OLIGOPEPTIDE;
PRION PROTEIN;
PROTEIN SUP35P;
TRANSLATION TERMINATION FACTOR;
UNCLASSIFIED DRUG;
ARTICLE;
CONFORMATIONAL TRANSITION;
GENE MUTATION;
NONHUMAN;
PRIORITY JOURNAL;
PROTEIN CONFORMATION;
PROTEIN DENATURATION;
PROTEIN PURIFICATION;
PROTEIN STRUCTURE;
SACCHAROMYCES CEREVISIAE;
TEMPERATURE SENSITIVITY;
AMYLOIDOSIS;
FUNGAL PROTEINS;
MOLECULAR CHAPERONES;
MUTATION;
OLIGOPEPTIDES;
OSMOLAR CONCENTRATION;
PLIABILITY;
PRIONS;
PROTEIN BIOSYNTHESIS;
PROTEIN DENATURATION;
PROTEIN STRUCTURE, QUATERNARY;
PROTEIN STRUCTURE, SECONDARY;
REPETITIVE SEQUENCES, AMINO ACID;
SACCHAROMYCES CEREVISIAE;
SACCHAROMYCES CEREVISIAE PROTEINS;
SOLUBILITY;
TEMPERATURE;
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EID: 0034758487
PISSN: 10728368
EISSN: None
Source Type: Journal
DOI: 10.1038/nsb1101-958 Document Type: Article |
Times cited : (94)
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References (30)
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