Role of the heat shock response and molecular chaperones in oncogenesis and cell death.
By C. Jolly, Richard I. Morimoto. Journal of the National Cancer Institute, 2000
1,102 citations recorded by the source corpus.
Subfields: Cell Biology, Materials Chemistry, Molecular Biology
View Paper: https://www.semanticscholar.org/paper/c1d2f8d294cf9461f1a9b493ff2ee46fe8cbc9c4
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In Cell Biology
In Materials Chemistry
In Molecular Biology
- J. Buchner
- L. Whitesell
- Susan Lindquist
- N. Holbrook
- J. Martindale
- Richard I. Morimoto
- R. Kaufman
- Shaloam Dasari
Citations in the corpus
- Heat shock factor 1 is a powerful multifaceted modifier of carcinogenesis. (2007, background): “Further, HSP70 and other chaperones interface with the apoptotic machinery with important functional consequences (Jolly and Morimoto, 2000).”
- HSP90 and the chaperoning of cancer (2005, background): “Several detailed reviews are available that address the molecular and cellular biology of the heat-shock respons”
- Necrosis: a specific form of programmed cell death? (2003, background): “The most studied of them are Hsp70 and Hsp27, which can inhibit apoptosis caused by various stimuli (heat shock, oxidative stress, ischemia/reperfusion, TNF, UV, anticancer drugs, and others) ([111,112]).”
- Role of Heat Shock Proteins in Livestock Adaptation to Heat Stress (2017, background): “In Saccharomyces cerevisiae, Caenorhabditiselegans, and Drosophila, only a single HSF is expressed, whereas al teast four members of HSF gene family get expressed in vertebrates and plants and three HSFs (HSF1, HSF2, and HSF4) has been characterized in humans [39,40].”
- Cellular response to oxidative stress: Signaling for suicide and survival * (2002, background): “Elevations in heat shock protein expression, particularly Hsp70 and the small heat shock proteins, have been shown to enhance survival of cells and prevent apoptosis during a wide variety of stress conditions (Jolly and Morimoto, 2000; Creagh et al., 2000a).”
- Hsp70 and Hsp90--a relay team for protein folding. (2004, background): “Compared to other chaperones, a wide variety of in vivo substrates is known for the Hsp70/Hsp90 chaperone network (Table 1) (Buchner 1999; Jolly and Morimoto 2000; Mayer et al. 2001; Picard 2002; Pratt and Toft 1997; Richter and Buchner 2001; Smith and Toft 1993; Walter and Buchner 2002; Young et…”