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  1. 1.   A novel ATP-dependent conformation in p97 N-D1 fragment revealed by crystal structures of disease-related mutants
  2. Tang, W. K.; Li, D. Y.; Li, C. C.; Esser, L.; Dai, R. M.; Guo, L. A.; Xia, D.
  3. Embo Journal. 2010, Jul; 29(13): 2217-2229.
  1. 2.   Multifunctional roles of the conserved arg residues in the second region of homology of p97/valosin-containing protein
  2. Wang, Q.; Song, C. C.; Irizarry, L.; Dai, R. M.; Zhang, X. D.; Li, C. C. H.
  3. Journal of Biological Chemistry. 2005, DEC 9; 280(49): 40515-40523.
  1. 3.   Molecular perspectives on p97-VCP: progress in understanding its structure and diverse biological functions
  2. Wang, Q.; Song, C. C.; Li, C. C. H.
  3. Journal of Structural Biology. 2004, APR-MAY; 146(1-2): 44-57.
  1. 4.   Hexamerization of p97-VCP is promoted by ATP binding to the D1 domain and required for ATPase and biological activities
  2. Wang, Q.; Song, C. C.; Li, C. C. H.
  3. Biochemical and Biophysical Research Communications. 2003 300(2): 253-260.
  1. 5.   D1 ring is stable and nucleotide-independent, whereas D2 ring undergoes major conformational changes during the ATPase cycle of p97-VCP
  2. Wang, Q.; Song, C. C.; Yang, X. Y.; Li, C. C. H.
  3. Journal of Biological Chemistry. 2003 278(35): 32784-32793.
  1. 6.   ATPase activity of p97-valosin-containing protein (VCP) - D2 mediates the major enzyme activity, and D1 contributes to the heat-induced activity
  2. Song, C. C.; Wang, Q.; Li, C. C. H.
  3. Journal of Biological Chemistry. 2003 278(6): 3648-3655.
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