Hsp31 is a stress response chaperone that intervenes in the protein misfolding process

Journal of Biological Chemistry

Volumn 290, Issue 41, 2015, Pages 24816-24834

  Tsai, Chai Jui ^a   Aslam, Kiran ^a   Drendel, Holli M ^a   Asiago, Josephat M ^a   Goode, Kourtney M ^a   Paul, Lake N ^b   Rochet, Jean Christophe ^a   Hazbun, Tony R ^a  

^a PURDUE UNIVERSITY   (United States)

^b PURDUE UNIVERSITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

AGGREGATES; SUBSTRATES; YEAST;

CHAPERONE ACTIVITY; FLUORESCENT PROTEIN; HEAT SHOCK PROTEIN; HOMODIMERIC PROTEINS; PROTECTIVE EFFECTS; PROTEIN MISFOLDING; PROTEOTOXIC STRESS; SUBSTRATE PROTEINS;

PROTEINS;

ALPHA SYNUCLEIN; CHAPERONE; CITRATE SYNTHASE; HEAT SHOCK PROTEIN; HEAT SHOCK PROTEIN 31; HYDROGEN PEROXIDE; INSULIN; LACTOYLGLUTATHIONE LYASE; PRION PROTEIN; UNCLASSIFIED DRUG; HSP31 PROTEIN, S CEREVISIAE; LACTIC ACID; METHYLGLYOXAL; PRION; PROTEIN AGGREGATE; REACTIVE OXYGEN METABOLITE; SACCHAROMYCES CEREVISIAE PROTEIN;

ARTICLE; AUTOPHAGY; CELL STRESS; CONTROLLED STUDY; CYTOPLASM; FUNGUS GROWTH; IN VITRO STUDY; NONHUMAN; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN ANALYSIS; PROTEIN DOMAIN; PROTEIN EXPRESSION; PROTEIN FOLDING; PROTEIN FUNCTION; PROTEIN MISFOLDING; SACCHAROMYCES CEREVISIAE; STOICHIOMETRY; YEAST; AMINO ACID SEQUENCE; CHEMISTRY; ENZYME ACTIVE SITE; HUMAN; METABOLISM; MOLECULAR GENETICS; OXIDATIVE STRESS; PRION; PROTEIN MULTIMERIZATION; PROTEIN QUATERNARY STRUCTURE;

ALPHA-SYNUCLEIN; AMINO ACID SEQUENCE; CATALYTIC DOMAIN; HEAT-SHOCK PROTEINS; HUMANS; LACTIC ACID; LACTOYLGLUTATHIONE LYASE; MOLECULAR SEQUENCE DATA; OXIDATIVE STRESS; PRIONS; PROTEIN AGGREGATES; PROTEIN FOLDING; PROTEIN MULTIMERIZATION; PROTEIN STRUCTURE, QUATERNARY; PYRUVALDEHYDE; REACTIVE OXYGEN SPECIES; SACCHAROMYCES CEREVISIAE; SACCHAROMYCES CEREVISIAE PROTEINS;

EID: 84943811273     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M115.678367     Document Type: Article

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