Phage P4 origin-binding domain structure reveals a mechanism for regulation of DNA-binding activity by homo- and heterodimerization of winged helix proteins-Reference-Cited by-同舟云学术

Phage P4 origin-binding domain structure reveals a mechanism for regulation of DNA-binding activity by homo- and heterodimerization of winged helix proteins

Published:2002-02 Issue:4 Volume:43 Page:855-867
ISSN:0950-382X
Container-title:Molecular Microbiology
language:en
Short-container-title:Mol Microbiol

Author:

Yeo Hye-Jeong,Ziegelin Gunter,Korolev Sergey,Calendar Richard,Lanka Erich,Waksman Gabriel

Publisher

Wiley

Subject

Molecular Biology,Microbiology

Link

http://onlinelibrary.wiley.com/wol1/doi/10.1046/j.1365-2958.2002.02796.x/fullpdf

Reference52 articles.

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2. KorB protein of promiscuous plasmid RP4 recognizes inverted sequence repetitions in regions essential for conjugative plasmid transfer

3. Functional synergy between DP-1 and E2F-1 in the cell cycle-regulating transcription factor DRTF1/E2F.

4. Crystal structure of the DNA-binding domain of the Epstein-Barr virus origin-binding protein EBNA1

5. A Method to Identify Protein Sequences That Fold into a Known Three-Dimensional Structure

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