The affinity of Ets-1 for DNA is modulated by phosphorylation through transient interactions of an unstructured region期刊界 All Journals 搜尽天下杂志传播学术成果专业期刊搜索期刊信息化学术搜索

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The affinity of Ets-1 for DNA is modulated by phosphorylation through transient interactions of an unstructured region

Authors:	Lee Gregory M Pufall Miles A Meeker Charles A Kang Hyun-Seo Graves Barbara J McIntosh Lawrence P

Institution:	¹ Department of Biochemistry and Molecular Biology, Department of Chemistry, and the Michael Smith Laboratories, University of British Columbia, Vancouver, BC, Canada V6T 1Z3 ² Department of Oncological Sciences, Huntsman Cancer Institute, University of Utah, Salt Lake City, UT 84312, USA

Abstract:

Keywords:	ATCUN amino-terminal copper and nickel-binding EMSA electrophoretic mobility-shift assay HSQC heteronuclear single quantum correlation HTH helix-turn-helix HX hydrogen exchange NOE nuclear Overhauser effect NOESY nuclear Overhauser effect spectroscopy PRE paramagnetic relaxation enhancement SRR serine-rich region (residues 244-301) SRR* truncated serine-rich region (residues 279-301) Ets-1 fragments are indicated by the boundaries of truncations from the N-terminus of the protein e g ΔN301 is a deletion of residues 1-300 and corresponds to Ets-1(301-440)
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