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Cited by 370

The DOI matches its Crossref record; 29 of the 29 references it cites were found in a registry or an index.

Purification and Properties of Drosophila Heat Shock Activator Protein

Wu, Carl, Wilson, Susan, Walker, Barbara, Dawid, Igor, Paisley, Thomas, Zimarino, Vincenzo, Ueda, Hitoshi·1987·Science

Abstract

Drosophila heat shock activator protein, a rare transacting factor which is induced upon heat shock to bind specifically to the heat shock regulatory sequence in vivo, has been purified from shocked cells to more than 95 percent homogeneity by sequence-specific duplex oligonucleotide affinity chromatography. The purified protein has a relative molecular mass of 110 kilodaltons, binds to the regulatory sequence with great affinity and specificity, and strongly stimulates transcription of the Drosophila hsp70 gene. Studies with this regulatory protein should lead to an understanding of the biochemical pathway underlying the heat shock phenomenon.

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Crossref · 10.1126/science.3685975

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Metadata

Authors
Wu, C., Wilson, S., Walker, B., Dawid, I., Paisley, T., Zimarino, V., & Ueda, H.
Venue
Science
Published
1987-11-27
Volume
238
Issue
4831
Pages
1247-1253
ISSN
  • 0036-8075 (ISSN-L)
  • 1095-9203
OpenAlex
W1980014349
Cited by
370
References
29
FWCI
17.57
Type
journal article
Language
en
Open access
closed

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CoChat. (2026). Citation check: Purification and Properties of Drosophila Heat Shock Activator Protein. https://app.cochat.ai/papers/10.1126/science.3685975
The paper
Wu, C., Wilson, S., Walker, B., Dawid, I., Paisley, T., Zimarino, V., & Ueda, H. (1987). Purification and Properties of Drosophila Heat Shock Activator Protein. Science. https://doi.org/10.1126/science.3685975

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Bibliographic data: Semantic Scholar, OpenAlex, Crossref.

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

Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.