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
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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Cites
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Self-citationA regulatory upstream promoter element in the Drosophila Hsp 70 heat-shock gene
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Cited by
Transcriptional Regulation in Mammalian Cells by Sequence-Specific DNA Binding Proteins
Mitchell, P. J., & Tjian, R. (1989) · Science · doi:10.1126/science.2667136 · Cited by 3,114
Sorger, P. K., & Pelham, H. R. B. (1988) · Cell · doi:10.1016/s0092-8674(88)91219-6 · Cited by 832
Dash, P. K., Hochner, B., & Kandel, E. R. (1990) · Nature · doi:10.1038/345718a0 · Cited by 744
Rougvie, A. E., & Lis, J. T. (1988) · Cell · doi:10.1016/s0092-8674(88)91087-2 · Cited by 666
Common DNA binding site for Fos protein complexesand transcription factor AP-1
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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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- 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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