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• W2020007236 startingPage "163" @default.
• W2020007236 abstract "Available data indicate that heat shock proteins act as chaperones under non-stress conditions by assisting in: (1) the folding of newly synthesized proteins, (2) the intracellular translocation of proteins, and (3) the function of other proteins. As we gain additional information concerning cellular physiology, we may find that heat shock proteins play a key role in many additional cellular functions. When cells experience thermal or chemical stress, heat shock proteins take on a new role, conserved from bacteria to humans, of protecting cells from the detrimental effects of stress. This latter role takes on added significance for the embryo in which the developmental program must be read linearly, with little opportunity to cycle backward to complete a missed segment of the program. Although circumstantial evidence clearly implicates heat shock proteins in protecting embryos from thermal stress, definitive evidence is still lacking. The challenge for the future is to obtain such definitive data. Ideally, such information will lead to new therapeutic paradigms that will afford protection to the human embryo/fetus exposed to thermal/chemical stress." @default.
• W2020007236 created "2016-06-24" @default.
• W2020007236 creator A5010768681 @default.
• W2020007236 date "1997-12-01" @default.
• W2020007236 modified "2023-10-18" @default.
• W2020007236 title "Molecular/cellular biology of the heat stress response and its role in agent-induced teratogenesis" @default.
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• W2020007236 doi "https://doi.org/10.1016/s0027-5107(97)00182-6" @default.
• W2020007236 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/9434867" @default.
• W2020007236 hasPublicationYear "1997" @default.
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