Title : Ordered assembly of heat shock proteins, Hsp26, Hsp70, Hsp90, and Hsp104, on expanded polyglutamine fragments revealed by chemical probes.

Pub. Date : 2011 Nov 25

PMID : 21969373






3 Functional Relationships(s)
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1 Ordered assembly of heat shock proteins, Hsp26, Hsp70, Hsp90, and Hsp104, on expanded polyglutamine fragments revealed by chemical probes. polyglutamine chaperone ATPase HSP104 Saccharomyces cerevisiae S288C
2 In Saccharomyces cerevisae, expanded polyglutamine (polyQ) fragments are assembled into discrete cytosolic aggregates in a process regulated by the molecular chaperones Hsp26, Hsp70, Hsp90, and Hsp104. polyglutamine chaperone ATPase HSP104 Saccharomyces cerevisiae S288C
3 In Saccharomyces cerevisae, expanded polyglutamine (polyQ) fragments are assembled into discrete cytosolic aggregates in a process regulated by the molecular chaperones Hsp26, Hsp70, Hsp90, and Hsp104. polyglutamine chaperone ATPase HSP104 Saccharomyces cerevisiae S288C