Mitochondrial Hsp78, a member of the Clp/Hsp100 family in Saccharomyces cerevisiae, cooperates with Hsp70 in protein refolding (Q73568734)

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5 November 2019

title

Mitochondrial Hsp78, a member of the Clp/Hsp100 family in Saccharomyces cerevisiae, cooperates with Hsp70 in protein refolding (English)

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5 November 2019

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Saccharomyces cerevisiae

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3

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5 November 2019

author name string

J Krzewska

series ordinal

1

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5 November 2019

T Langer

series ordinal

2

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5 November 2019

publication date

1 January 2001

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5 November 2019

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5 November 2019

volume

489

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5 November 2019

issue

1

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5 November 2019

page(s)

92-96

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HSP100/Clp proteins: a common mechanism explains diverse functions

5 November 2019

cites work

1 reference

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Posttranslational quality control: folding, refolding, and degrading proteins.

21 January 2018

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HSP104 required for induced thermotolerance

21 January 2018

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HSP78 encodes a yeast mitochondrial heat shock protein in the Clp family of ATP-dependent proteases

21 January 2018

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ClpB is the Escherichia coli heat shock protein F84.1.

21 January 2018

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Expression of ClpB, an analog of the ATP-dependent protease regulatory subunit in Escherichia coli, is controlled by a heat shock sigma factor (sigma 32).

21 January 2018

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A novel factor required for the assembly of the DnaK and DnaJ chaperones of Thermus thermophilus

21 January 2018

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Protein disaggregation mediated by heat-shock protein Hsp104.

21 January 2018

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Degradation by proteases Lon, Clp and HtrA, of Escherichia coli proteins aggregated in vivo by heat shock; HtrA protease action in vivo and in vitro.

21 January 2018

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Genetic evidence for a functional relationship between Hsp104 and Hsp70.

21 January 2018

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Hsp104, Hsp70, and Hsp40: a novel chaperone system that rescues previously aggregated proteins

21 January 2018

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Identification of thermolabile Escherichia coli proteins: prevention and reversion of aggregation by DnaK and ClpB.

21 January 2018

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Sequential mechanism of solubilization and refolding of stable protein aggregates by a bichaperone network

21 January 2018

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ClpB cooperates with DnaK, DnaJ, and GrpE in suppressing protein aggregation. A novel multi-chaperone system from Escherichia coli

21 January 2018

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Heat-inactivated proteins are rescued by the DnaK.J-GrpE set and ClpB chaperones

21 January 2018

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Heat-inactivated proteins managed by DnaKJ-GrpE-ClpB chaperones are released as a chaperonin-recognizable non-native form

21 January 2018

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The molecular chaperone Hsp78 confers compartment-specific thermotolerance to mitochondria

21 January 2018

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Role of the mitochondrial DnaJ homologue, Mdj1p, in the prevention of heat-induced protein aggregation.

21 January 2018

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Dual role of the mitochondrial chaperone Mdj1p in inheritance of mitochondrial DNA in yeast

21 January 2018

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Structure-function analyses of the Ssc1p, Mdj1p, and Mge1p Saccharomyces cerevisiae mitochondrial proteins in Escherichia coli

21 January 2018

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Purification and biochemical properties of Saccharomyces cerevisiae Mdj1p, the mitochondrial DnaJ homologue

21 January 2018

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Purification and biochemical properties of Saccharomyces cerevisiae's Mge1p, the mitochondrial cochaperone of Ssc1p.

21 January 2018

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Hsp78, a Clp homologue within mitochondria, can substitute for chaperone functions of mt-hsp70

21 January 2018

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A mitochondrial homolog of bacterial GrpE interacts with mitochondrial hsp70 and is essential for viability

7 January 2021

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DnaK, DnaJ and GrpE form a cellular chaperone machinery capable of repairing heat-induced protein damage.

7 January 2021

1 reference

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10.1016/S0014-5793(00)02423-6

7 January 2021

Identifiers

DOI

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5 November 2019

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