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Nature Reviews Molecular Cell Biology, 2019
The 70-kDa heat shock proteins (Hsp70s) are ubiquitous molecular chaperones that act in a large variety of cellular protein folding and remodelling processes. They function virtually at all stages of the life of proteins from synthesis to degradation and are thus crucial for maintaining protein homeostasis, with direct implications for human health.
Rina Rosenzweig +3 more
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The 70-kDa heat shock proteins (Hsp70s) are ubiquitous molecular chaperones that act in a large variety of cellular protein folding and remodelling processes. They function virtually at all stages of the life of proteins from synthesis to degradation and are thus crucial for maintaining protein homeostasis, with direct implications for human health.
Rina Rosenzweig +3 more
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Recent Patents on DNA & Gene Sequences, 2011
Hsp70 classes of molecular chaperones are highly conserved in all organisms and play an essential role in the maintenance of cellular homeostasis. Hsp70s assist nascent chain protein folding and denatured proteins, as well as the import of proteins to the organelles, and solubilization of aggregated proteins.
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Hsp70 classes of molecular chaperones are highly conserved in all organisms and play an essential role in the maintenance of cellular homeostasis. Hsp70s assist nascent chain protein folding and denatured proteins, as well as the import of proteins to the organelles, and solubilization of aggregated proteins.
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Experientia, 1994
Numerous reports suggest that stress protein accumulation confers protection in various mammalian tissues against differing stresses. The purpose of this article is to review the evidence that stress proteins, in particular hsp70, are able to alter the resistance of the heart to subsequent ischaemic and non-ischaemic injury and to discuss the possible ...
D M, Yellon, M S, Marber
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Numerous reports suggest that stress protein accumulation confers protection in various mammalian tissues against differing stresses. The purpose of this article is to review the evidence that stress proteins, in particular hsp70, are able to alter the resistance of the heart to subsequent ischaemic and non-ischaemic injury and to discuss the possible ...
D M, Yellon, M S, Marber
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2001
Publisher Summary This chapter describes the molecular basis of Hsp70 chaperone machines. Particular emphasis is given to the DnaK system of Escherichia coli as it is the best understood Hsp70 system, and to the mechanistic differences between Hsp70 family members.
Mayer, Matthias P. +3 more
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Publisher Summary This chapter describes the molecular basis of Hsp70 chaperone machines. Particular emphasis is given to the DnaK system of Escherichia coli as it is the best understood Hsp70 system, and to the mechanistic differences between Hsp70 family members.
Mayer, Matthias P. +3 more
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Hsp70s and lysosomal proteolysis
Experientia, 1994Confluent cultured cells activate a lysosomal pathway of polypeptide breakdown in response to withdrawal of serum growth factors. The substrates for this proteolytic pathway are a restricted class of cytosolic polypeptides containing peptide sequences biochemically related to lysine-phenylalanine-glutamate-arginine-glutamine, or, in single amino acid ...
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2013
Hsp70 proteins function as ATP-dependent molecular chaperones, which are involved in the folding of newly synthesized polypeptides, the assembly of multi-protein complexes and the transport of proteins across cellular membranes. Hsp70 is crucial for maintaining protein homeostasis, thus disregulation of Hsp70 is found in many human diseases, such as ...
Yaoyu Chen, Wenlai Zhou
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Hsp70 proteins function as ATP-dependent molecular chaperones, which are involved in the folding of newly synthesized polypeptides, the assembly of multi-protein complexes and the transport of proteins across cellular membranes. Hsp70 is crucial for maintaining protein homeostasis, thus disregulation of Hsp70 is found in many human diseases, such as ...
Yaoyu Chen, Wenlai Zhou
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Hsp70 Escort Protein: More Than a Regulator of Mitochondrial Hsp70
Current Proteomics, 2018Hsp70 members occupy a central role in proteostasis and are found in different eukaryotic cellular compartments. The mitochondrial Hsp70/J-protein machinery performs multiple functions vital for the proper functioning of the mitochondria, including forming part of the import motor that transports proteins from the cytosol into the matrix and inner ...
David O. Nyakundi +2 more
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Interaction of Hsp70 chaperones with substrates
Nature Structural & Molecular Biology, 1997Determination of the structure of the substrate binding domain of the Escherichia coli Hsp70 chaperone, DnaK, and the biochemical characterisation of the motif it recognizes within substrates provide insights into the principles governing Hsp70 interaction with polypeptide chains.
Rüdiger, Stefan +2 more
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2013
Aging or senescence in biology is defined as the process of gradual loss of important body functions and cells, and in particular, the inability of cells to reproduce and cope with stress. Important features of an aging cell include the progressive accumulation of damaged proteins, abnormal protein aggregates and oxidative stress.
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Aging or senescence in biology is defined as the process of gradual loss of important body functions and cells, and in particular, the inability of cells to reproduce and cope with stress. Important features of an aging cell include the progressive accumulation of damaged proteins, abnormal protein aggregates and oxidative stress.
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Hsp70 proteins in protein translocation
2001Publisher Summary Hsp70 proteins are essential components of the protein translocation systems of the endoplasmic reticulum (ER) and mitochondria. The role of Hsp70s in protein translocation is not confined to the ER and mitochondria. For most proteins of the ER, translocation is coupled with protein synthesis.
Ryan, Michael T., Pfanner, Nikolaus
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