Single methyl group determines prion propagation and protein degradation activities of yeast heat shock protein (Hsp)-70 chaperones Ssa1p and Ssa2p

Proceedings of the National Academy of Sciences of the United States of America

Volumn 108, Issue 33, 2011, Pages 13665-13670

  Sharma, Deepak ^a   Masison, Daniel C ^a  

^a NATIONAL INSTITUTE OF DIABETES AND DIGESTIVE AND KIDNEY DISEASES   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ALANINE; CELL PROTEIN; CHAPERONE; GLYCINE; HEAT SHOCK PROTEIN 70; PRION PROTEIN; PROTEIN SSA1P; PROTEIN SSA2P; UNCLASSIFIED DRUG;

ARTICLE; ENZYME ACTIVITY; GLUCONEOGENESIS; PRIORITY JOURNAL; PROTEIN DEGRADATION; PROTEIN FOLDING; PROTEIN FUNCTION; SEQUENCE HOMOLOGY;

ADENOSINE TRIPHOSPHATASES; AMINO ACID SEQUENCE; BINDING SITES; HSP70 HEAT-SHOCK PROTEINS; METHYLATION; MUTAGENESIS, SITE-DIRECTED; PRIONS; PROTEIN BINDING; SACCHAROMYCES CEREVISIAE; SACCHAROMYCES CEREVISIAE PROTEINS;

EID: 80052010587     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1107421108     Document Type: Article

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