Hydroxycarboxylic Acid Receptor 2 Mediates β‐hydroxybutyrate's Antiseizure Effect in Mice
A Objective The ketogenic diet, a high‐fat, low‐carbohydrate regimen, is often used to treat drug‐resistant seizures and is being studied for Alzheimer's disease and other neuropsychiatric disorders. However, its mechanism of action remains unclear. β‐hydroxybutyrate, a primary circulating ketone body produced by the ketogenic diet, may mediate its ...
Soudabeh Naderi +10 more
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Heat shock protein gene expression varies among populations but does not strongly track recent environmental conditions: implications for biomarker development. [PDF]
Woodruff MJ +5 more
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Structural basis for the allosteric activation of Lon by the heat shock protein LarA. [PDF]
Wang HJ, Kuan YE, Ho MR, Chang CI.
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The enigma of small heat shock protein phosphorylation. [PDF]
Gaestel M.
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<i>Acanthospermum australe</i> Extract Inhibits the Chaperone Activity of <i>Plasmodium falciparum</i> Heat Shock Protein 70-1. [PDF]
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Activation mechanism of small heat shock protein HSPB5 revealed by disease-associated mutants. [PDF]
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Legume lectin phytohemagglutinin reduces transepithelial electrical resistance by counteracting the chaperone function of heat shock protein-70. [PDF]
Dokladny K, Setty P, Moseley PL, Lin HC.
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AbstractHeat‐shock proteins (HSPs), or stress proteins, are abundant and highly conserved, present in all organisms and in all cells. Selected HSPs, also known as chaperones, play crucial roles in folding and unfolding of proteins, assembly of multiprotein complexes, transport and sorting of proteins into correct subcellular compartments, cell‐cycle ...
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Abstract Bacteria, plans and animals are all very sensitive to small changes of temperature and, indeed, life of any sort is possible only within a relatively small temperature range. Although it is well established that heat stress induces tolerance to further heat stress, the nature of the response at the molecular level has been obscure.
S, Lindquist, E A, Craig
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AbstractHeat‐shock proteins (HSPs), or stress proteins, are highly conserved and present in all organisms and in all cells of all organisms. Selected HSPs, also known as chaperones, play crucial roles in folding/unfolding of proteins, assembly of multiprotein complexes, transport/sorting of proteins into correct subcellular compartments, cell‐cycle ...
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