Interaction of heat shock protein 90 and the co-chaperone Cpr6 with Ura2, a bifunctional enzyme required for pyrimidine biosynthesis
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The Hsp90 cochaperones Cpr6, Cpr7, and Cns1 interact with the intact ribosomeAn Hsp90 co-chaperone protein in yeast is functionally replaced by site-specific posttranslational modification in humansHsp90-Associated Immunophilin Homolog Cpr7 Is Required for the Mitotic Stability of [URE3] Prion in Saccharomyces cerevisiae.Hsp104 disaggregase at normal levels cures many [PSI+] prion variants in a process promoted by Sti1p, Hsp90, and Sis1p.Evidence for Hsp90 Co-chaperones in Regulating Hsp90 Function and Promoting Client Protein Folding.Mutation of essential Hsp90 co-chaperones SGT1 or CNS1 renders yeast hypersensitive to overexpression of other co-chaperones.
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Interaction of heat shock protein 90 and the co-chaperone Cpr6 with Ura2, a bifunctional enzyme required for pyrimidine biosynthesis
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article científic
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article scientifique
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articolo scientifico
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artigo científico
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bilimsel makale
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scientific article published on 07 August 2013
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vedecký článok
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vetenskaplig artikel
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videnskabelig artikel
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vědecký článek
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Interaction of heat shock prot ...... ed for pyrimidine biosynthesis
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Interaction of heat shock prot ...... d for pyrimidine biosynthesis.
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Interaction of heat shock prot ...... ed for pyrimidine biosynthesis
@en
Interaction of heat shock prot ...... d for pyrimidine biosynthesis.
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Interaction of heat shock prot ...... ed for pyrimidine biosynthesis
@en
Interaction of heat shock prot ...... d for pyrimidine biosynthesis.
@nl
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P356
P1476
Interaction of heat shock prot ...... ed for pyrimidine biosynthesis
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Jill L Johnson
Nicholas Wren
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P304
27406-27414
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10.1074/JBC.M113.504142
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P577
2013-08-07T00:00:00Z