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  1. 1.   The importance of Raf dimerization in cell signaling
  2. Freeman, A. K.; Ritt, D. A.; Morrison, D. K.
  3. Small GTPases. 2013, Jul-Sep; 4(3): 180-5.
  1. 2.   Proteomic analysis of scaffold proteins in the ERK cascade
  2. McKay, M. M.; Morrison, D. K.
  3. Methods in molecular biology (Clifton, N.J.). 2010 661: 323-34.
  1. 3.   Signaling dynamics of the KSR1 scaffold complex
  2. McKay, M. M.; Ritt, D. A.; Morrison, D. K.
  3. Proceedings of the National Academy of Sciences of the United States of America. 2009, Jul 7; 106(27): 11022-7.
  1. 4.   KSR2 is a calcineurin substrate that promotes ERK cascade activation in response to calcium signals
  2. Dougherty, M. K.; Ritt, D. A.; Zhou, M.; Specht, S. I.; Monson, D. M.; Veenstra, T. D.; Morrison, D. K.
  3. Molecular Cell. 2009, Jun 26; 34(6): 652-62.
  1. 5.   Coactivators and corepressors of NF-kappa B in I kappa Beta alpha gene promoter
  2. Gao, Z. G.; Chiao, P.; Zhang, X.; Zhang, X. H.; Lazar, M. A.; Seto, E.; Young, H. A.; Ye, J. P.
  3. Journal of Biological Chemistry. 2005, JUN 3; 280(22): 21091-21098.
  1. 6.   Alternative p38 activation pathway mediated by T cell receptor-proximal tyrosine kinases
  2. Salvador, J. M.; Mittelstadt, P. R.; Guszczynski, T.; Copeland, T. D.; Yamaguchi, H.; Appella, E.; Fornace, A. J.; Ashwell, J. D.
  3. Nature Immunology. 2005 6(4): 390-395.
  1. 7.   Osteopontin regulation by inorganic phosphate is ERK1/2-, protein kinase C-, and proteasome-dependent
  2. Beck, G. R.; Knecht, N.
  3. Journal of Biological Chemistry. 2003 278(43): 41921-41929.
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