Purification and Properties of Drosophila Heat Shock Activator Protein.

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Title: Purification and Properties of Drosophila Heat Shock Activator Protein.
Authors: WU, CARL (AUTHOR), WILSON, SUSAN (AUTHOR), WALKER, BARBARA (AUTHOR), DAWID, IGOR (AUTHOR), PAISLEY, THOMAS (AUTHOR), ZIMARINO, VINCENZO (AUTHOR), UEDA, HITOSHI (AUTHOR)
Source: Science (pre-March 2025). 11/27/1987, Vol. 238 Issue 4831, p1247-1253. 7p. 1 Diagram, 5 Graphs.
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. [ABSTRACT FROM AUTHOR]
Copyright of Science (pre-March 2025) is the property of American Association for the Advancement of Science and its content may not be copied or emailed to multiple sites without the copyright holder's express written permission. Additionally, content may not be used with any artificial intelligence tools or machine learning technologies. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.)
Database: Psychology and Behavioral Sciences Collection
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  Data: Purification and Properties of Drosophila Heat Shock Activator Protein.
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  Data: <searchLink fieldCode="AR" term="%22WU%2C+CARL%22">WU, CARL</searchLink> (AUTHOR)<br /><searchLink fieldCode="AR" term="%22WILSON%2C+SUSAN%22">WILSON, SUSAN</searchLink> (AUTHOR)<br /><searchLink fieldCode="AR" term="%22WALKER%2C+BARBARA%22">WALKER, BARBARA</searchLink> (AUTHOR)<br /><searchLink fieldCode="AR" term="%22DAWID%2C+IGOR%22">DAWID, IGOR</searchLink> (AUTHOR)<br /><searchLink fieldCode="AR" term="%22PAISLEY%2C+THOMAS%22">PAISLEY, THOMAS</searchLink> (AUTHOR)<br /><searchLink fieldCode="AR" term="%22ZIMARINO%2C+VINCENZO%22">ZIMARINO, VINCENZO</searchLink> (AUTHOR)<br /><searchLink fieldCode="AR" term="%22UEDA%2C+HITOSHI%22">UEDA, HITOSHI</searchLink> (AUTHOR)
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  Data: <searchLink fieldCode="JN" term="%22Science+%28pre-March+2025%29%22">Science (pre-March 2025)</searchLink>. 11/27/1987, Vol. 238 Issue 4831, p1247-1253. 7p. 1 Diagram, 5 Graphs.
– Name: Abstract
  Label: Abstract
  Group: Ab
  Data: 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. [ABSTRACT FROM AUTHOR]
– Name: AbstractSuppliedCopyright
  Label:
  Group: Ab
  Data: <i>Copyright of Science (pre-March 2025) is the property of American Association for the Advancement of Science and its content may not be copied or emailed to multiple sites without the copyright holder's express written permission. Additionally, content may not be used with any artificial intelligence tools or machine learning technologies. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract.</i> (Copyright applies to all Abstracts.)
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        Value: 10.1126/science.3685975
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        Text: English
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            NameFull: WILSON, SUSAN
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            NameFull: WALKER, BARBARA
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            NameFull: PAISLEY, THOMAS
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              Text: 11/27/1987
              Type: published
              Y: 1987
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              Value: 4831
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