ArticleMolecular and cellular biology1988
The major inducible heat shock protein hsp68 is not required for acquisition of thermal resistance in mouse plasmacytoma cell lines.
Article in Molecular and cellular biology, 1988. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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4 citing papers in PubMed, 29 citations in OpenAlex.
- Article
- Downstream caspases are novel targets for the antiapoptotic activity of the molecular chaperone hsp70.Cell stress & chaperones · 2004Article
- Hsp104 is required for tolerance to many forms of stress.The EMBO journal · 1992Article
- Characterization of the heat shock response in cultured sugarcane cells : I. Physiology of the heat shock response and heat shock protein synthesis.Plant physiology · 1989Article
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2 authors at 1 institution in 1 country.
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Abstract
In mouse cells, the major inducible heat shock protein is a protein of 68,000 daltons (hsp68). We have previously shown that mouse plasmacytomas do not express hsp68. We have now made use of these natural mutants to assess the contribution of hsp68 to acquired thermotolerance. An endpoint limiting dilution assay was used to quantify cell survival to lethal stresses. Two test plasmacytoma cell lines (C1.18.1 and J558) and an hsp68-positive myeloma, XC1.1/51, used as a control, were examined. All showed recovery when pretreated for 10 min at 44 degrees C 2 h before exposure to otherwise lethal stresses of 1 to 4 h at 43 degrees C. Similar results were obtained with the Friend erythroleukemia line D1B, which we have also shown not to express hsp68. These results indicate that hsp68 is not required for protection against thermal stresses in mouse cells.
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