ArticleNucleic acids research1994
Heat shock-induced repression of proteolysis: poly(A)-binding protein degradation patterns can illusorily suggest its specific loss during heat shock.
Article in Nucleic acids research, 1994. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.
What it found
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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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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
2 citing papers in PubMed, 9 citations in OpenAlex.
- Rapamycin conditionally inhibits Hsp90 but not Hsp70 mRNA translation in Drosophila: implications for the mechanisms of Hsp mRNA translation.Cell stress & chaperones · 2008Article
- Levels of free PABP are limited by newly polyadenylated mRNA in early Spisula embryogenesis.Nucleic acids research · 2000Article
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Poly(A)-binding protein (PABP) is highly susceptible to proteolysis during cell lysis of Drosophila tissue culture cells unless substantial amounts of proteolysis inhibitors are included in the extraction buffer. This intrinsic proteolytic activity is substantially reduced during heat shock. An artifactual appearance that poly(A)-binding protein is specifically degraded by heat shock can result. Several contradictory descriptions of PABP may also be related to its proteolysis. Repression of proteolysis is likely to reflect a physiologically significant regulatory event, based on recent examinations of HSP70 stability during and after heat shock.
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