Phosphorylation and Stabilization of Topoisomerase IIα Protein by p38γ Mitogen-activated Protein Kinase Sensitize Breast Cancer Cells to Its Poisons

Lignende værker

• p38γ Mitogen-activated Protein Kinase Signals through Phosphorylating Its Phosphatase PTPH1 in Regulating Ras Protein Oncogenesis and Stress Response
  af: Hou, Songwang, et al.
  Udgivet: (2012)
• p38γ Mitogen-activated Protein Kinase (MAPK) Confers Breast Cancer Hormone Sensitivity by Switching Estrogen Receptor (ER) Signaling from Classical to Nonclassical Pathway via Stimulating ER Phosphorylation and c-Jun Transcription
  af: Qi, Xiaomei, et al.
  Udgivet: (2012)
• The K-Ras effector p38γ MAPK confers intrinsic resistance to tyrosine kinase inhibitors by stimulating EGFR transcription and EGFR dephosphorylation
  af: Yin, Ning, et al.
  Udgivet: (2017)
• Molecular Basis of the Interaction of the Human Protein Tyrosine Phosphatase Non-receptor Type 4 (PTPN4) with the Mitogen-activated Protein Kinase p38γ
  af: Maisonneuve, Pierre, et al.
  Udgivet: (2016)
• p38γ MAPK Cooperates with c-Jun in trans-Activating Matrix Metalloproteinase 9
  af: Loesch, Mathew, et al.
  Udgivet: (2010)