Now showing items 1-2 of 2

    • MK2 Phosphorylates RIPK1 to Prevent TNF-Induced Cell Death. 

      Jaco, I; Annibaldi, A; Lalaoui, N; Wilson, R; Tenev, T; Laurien, L; Kim, C; Jamal, K; Wicky John, S; Liccardi, G; Chau, D; Murphy, JM; Brumatti, G; Feltham, R; Pasparakis, M; Silke, J; Meier, P (2017-06)
      TNF is an inflammatory cytokine that upon binding to its receptor, TNFR1, can drive cytokine production, cell survival, or cell death. TNFR1 stimulation causes activation of NF-κB, p38α, and its downstream effector kinase ...
    • Ubiquitin-Mediated Regulation of RIPK1 Kinase Activity Independent of IKK and MK2. 

      Annibaldi, A; Wicky John, S; Vanden Berghe, T; Swatek, KN; Ruan, J; Liccardi, G; Bianchi, K; Elliott, PR; Choi, SM; Van Coillie, S; Bertin, J; Wu, H; Komander, D; Vandenabeele, P; Silke, J; Meier, P (2018-02)
      Tumor necrosis factor (TNF) can drive inflammation, cell survival, and death. While ubiquitylation-, phosphorylation-, and nuclear factor κB (NF-κB)-dependent checkpoints suppress the cytotoxic potential of TNF, it remains ...