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Cited by 277

The DOI matches its Crossref record; 24 of the 24 references it cites were found in a registry or an index.

Heat shock-induced translational alterations in HeLa cells. Initiation factor modifications and the inhibition of translation.

Open access
Duncan, R, Hershey, J W·1984·Journal of Biological Chemistry

Abstract

Heat shock at 45 degrees C virtually abolishes protein synthesis in HeLa cells, but return to 37 degrees C effects a complete recovery and the concomitant synthesis of heat shock-induced proteins. Heat shock induces polysome disaggregation, indicating initiation is principally inhibited. In vitro assays for initiation factor activities reveal heat shock inhibits eukaryotic initiation factor 2 (eIF-2), eIF-(3 + 4F), and eIF-4B. Immunoblot analyses show that eIF-2 alpha and eIF-2 beta become modified during heat shock, and eIF-4B variants disappear. Upon return to 37 degrees C, these alterations reverse. The modifications of eIF-2 alpha and eIF-4B are due to phosphorylation and dephosphorylation, respectively. Enzymatic activities induced by heat shock inhibit protein synthesis and modify initiation factors in a rabbit reticulocyte lysate. Initiation factor modifications may contribute to, or cause, protein synthesis inhibition.

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Metadata

Authors
Duncan, R., & Hershey, J. W.
Venue
Journal of Biological Chemistry
Publisher
Elsevier BV
Published
1984-10
Volume
259
Issue
19
Pages
11882-11889
ISSN
0021-9258 (ISSN-L)
OpenAlex
W1506260722
Cited by
277
References
24
FWCI
9.04
Type
journal article
Language
en
Open access
hybrid

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CoChat. (2026). Citation check: Heat shock-induced translational alterations in HeLa cells. Initiation factor modifications and the inhibition of translation. https://app.cochat.ai/papers/10.1016/s0021-9258(20)71294-9
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Duncan, R., & Hershey, J. W. (1984). Heat shock-induced translational alterations in HeLa cells. Initiation factor modifications and the inhibition of translation. Journal of Biological Chemistry. https://doi.org/10.1016/s0021-9258(20)71294-9

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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).

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