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Behind the Fos and Jun leucine zipper.

作者信息

Kouzarides T, Ziff E

机构信息

Department of Biochemistry, Kaplan Cancer Center, N.Y. University Medical Center, New York 10016.

出版信息

Cancer Cells. 1989 Nov;1(3):71-6.

PMID:2518283
Abstract

The production of the nuclear oncoproteins Fos and Jun is rapidly induced in response to extracellular signals. In the nucleus, the two proteins combine to form a tight complex via leucine zipper domains. The resulting Fos-Jun heterodimer can bind to the TPA-responsive element (TRE) by way of a novel, highly basic motif and can activate the transcription of TPA-responsive genes. The existence of several Fos- and Jun-related proteins with dimerization and DNA binding properties similar to Fos and Jun suggests that these two oncoproteins may be part of a network of related but functionally distinct transcription factors.

摘要

相似文献

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Behind the Fos and Jun leucine zipper.
Cancer Cells. 1989 Nov;1(3):71-6.
2
Analysis of dimerization and DNA binding functions in Fos and Jun by domain-swapping: involvement of residues outside the leucine zipper/basic region.通过结构域交换分析Fos和Jun中的二聚化及DNA结合功能:亮氨酸拉链/碱性区域之外残基的作用
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Nature. 1989 Sep 21;341(6239):243-5. doi: 10.1038/341243a0.
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Changing fos oncoprotein to a jun-independent DNA binding protein with GCN4 dimerization specificity by swapping "leucine zippers".通过交换“亮氨酸拉链”将原癌基因蛋白fos转变为具有GCN4二聚化特异性的不依赖于jun的DNA结合蛋白。
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Oncogene. 2000 Mar 30;19(14):1752-63. doi: 10.1038/sj.onc.1203491.

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