Modulation of replication protein A function by its hyperphosphorylation-induced conformational change involving DNA binding domain B.

@article{Liu2005ModulationOR,
  title={Modulation of replication protein A function by its hyperphosphorylation-induced conformational change involving DNA binding domain B.},
  author={Yiyong Liu and Mamuka Kvaratskhelia and Sonja Hess and Youxing Qu and Yue Zou},
  journal={The Journal of biological chemistry},
  year={2005},
  volume={280 38},
  pages={
          32775-83
        }
}
Human replication protein A (RPA), composed of RPA70, RPA32, and RPA14 subunits, undergoes hyperphosphorylation in cells in response to DNA damage. Hyperphosphorylation that occurs predominately in the N-terminal region of RPA32 is believed to play a role in modulating the cellular activities of RPA essential for almost all DNA metabolic pathways. To understand how the hyperphosphorylation modulates the functions of RPA, we compared the structural characteristics of full-length native and… CONTINUE READING

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NUMBER 38 JOURNAL OF BIOLOGICAL CHEMISTRY 32783 by gest on July 13

Y. Lao, X. V. Gomes, Y. Ren, J. S. Taylor, M. S. Wold
  • Hyperphosphorylation-induced Conformational Change of RPA SEPTEMBER
  • 2005
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