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Experientia, 1994
An alteration in the ability of cells to express heat shock proteins could be physiologically important in aging because all living organisms show a reduced ability to respond to stress with increasing age. Using hepatocytes freshly isolated from young adult and old rats, we have shown that the induction of hsp70 expression by heat shock is reduced ...
A R, Heydari +4 more
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An alteration in the ability of cells to express heat shock proteins could be physiologically important in aging because all living organisms show a reduced ability to respond to stress with increasing age. Using hepatocytes freshly isolated from young adult and old rats, we have shown that the induction of hsp70 expression by heat shock is reduced ...
A R, Heydari +4 more
openaire +2 more sources
Hsp70 in cancer: A double agent in the battle between survival and death
Journal of Cellular Physiology, 2020The heat shock protein (Hsps) superfamily, also known as molecular chaperones, are highly conserved and present in all living organisms and play vital roles in protein fate.
Mehdi Asghari Vostakolaei +5 more
semanticscholar +1 more source
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
openaire +3 more sources
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
openaire +2 more sources
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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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
Chemokines are signaling molecules that regulate cell migration and are considered as molecules of major biological importance both in physiological and pathological conditions. Given their significance, recombinant chemokines have become valuable research/diagnostic and therapeutic tools.
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Chemokines are signaling molecules that regulate cell migration and are considered as molecules of major biological importance both in physiological and pathological conditions. Given their significance, recombinant chemokines have become valuable research/diagnostic and therapeutic tools.
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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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Nature Structural & Molecular Biology, 2005
Recent studies show that Hsp70 chaperones associate with ribosomes not only in yeast but also in humans. Differences seem to exist among species regarding the identities of Hsp70 homologs involved as well as the mechanisms of their ribosomal recruitment and activation.
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Recent studies show that Hsp70 chaperones associate with ribosomes not only in yeast but also in humans. Differences seem to exist among species regarding the identities of Hsp70 homologs involved as well as the mechanisms of their ribosomal recruitment and activation.
openaire +1 more source