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Hsp70 chaperones: Cellular functions and molecular mechanism
  • M. Mayer, B. Bukau
  • Biology, Medicine
  • Cellular and Molecular Life Sciences
  • 1 March 2005
Abstract.Hsp70 proteins are central components of the cellular network of molecular chaperones and folding catalysts. They assist a large variety of protein folding processes in the cell by transientExpand
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The Hsp70 and Hsp60 Chaperone Machines
B. B. thanks members of his lab and J. Reinstein for critical reading of the manuscript and C. Gassler, T. Laufen, and S. Rudiger for figure preparation. A. H. thanks Wayne Fenton for criticalExpand
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Molecular Chaperones and Protein Quality Control
In living cells, both newly made and preexisting polypeptide chains are at constant risk for misfolding and aggregation. In accordance with the wide diversity of misfolded forms, elaborateExpand
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Substrate specificity of the DnaK chaperone determined by screening cellulose‐bound peptide libraries
Hsp70 chaperones assist protein folding by ATP‐dependent association with linear peptide segments of a large variety of folding intermediates. The molecular basis for this ability to differentiateExpand
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Cellular strategies for controlling protein aggregation
The aggregation of misfolded proteins is associated with the perturbation of cellular function, ageing and various human disorders. Mounting evidence suggests that protein aggregation is often partExpand
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Mechanism of regulation of hsp70 chaperones by DnaJ cochaperones.
Hsp70 chaperones assist a large variety of protein folding processes within the entire lifespan of proteins. Central to these activities is the regulation of Hsp70 by DnaJ cochaperones. DnaJExpand
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Selective Ribosome Profiling Reveals the Cotranslational Chaperone Action of Trigger Factor In Vivo
As nascent polypeptides exit ribosomes, they are engaged by a series of processing, targeting, and folding factors. Here, we present a selective ribosome profiling strategy that enables globalExpand
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Hsp42 is required for sequestration of protein aggregates into deposition sites in Saccharomyces cerevisiae
The budding yeast heat shock protein Hsp42 coaggregates with misfolded proteins and may link those aggregates to further sorting factors.
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Identification of thermolabile Escherichia coli proteins: prevention and reversion of aggregation by DnaK and ClpB
We systematically analyzed the capability of the major cytosolic chaperones of Escherichia coli to cope with protein misfolding and aggregation during heat stress in vivo and in cell extracts. UnderExpand
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Chaperone network in the yeast cytosol: Hsp110 is revealed as an Hsp70 nucleotide exchange factor
The Hsp110 proteins, exclusively found in the eukaryotic cytosol, have significant sequence homology to the Hsp70 molecular chaperone superfamily. Despite this homology and the cellular abundance ofExpand
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