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  1. Article

    Vaccinia virus anti-apoptotic F1L is a novel Bcl-2-like domain-swapped dimer that binds a highly selective subset of BH3-containing death ligands

    Apoptosis is an important part of the host's defense mechanism for eliminating invading pathogens. Some viruses express proteins homologous in sequence and function to mammalian pro-survival Bcl-2 proteins. An...

    M Kvansakul, H Yang, W D Fairlie, P E Czabotar, S F Fischer in Cell Death & Differentiation (2008)

  2. Article

    Erratum: Modified vaccinia virus Ankara protein F1L is a novel BH3-domain-binding protein and acts together with the early viral protein E3L to block virus-associated apoptosis

    Correction to: Cell Death and Differentiation (2006) 13, 109–118. doi:10.1038/sj.cdd.4401718 It has come to our attention that a peptide sequence has been mislabelled in Figure 7 of this article. Inadvertently...

    S F Fischer, H Ludwig, J Holzapfel, M Kvansakul, L Chen in Cell Death & Differentiation (2008)

  3. Article

    CED-4 forms a 2 : 2 heterotetrameric complex with CED-9 until specifically displaced by EGL-1 or CED-13

    The pathway to cell death in Caenorhabditis elegans is well established. In cells undergoing apoptosis, the Bcl-2 homology domain 3 (BH3)-only protein EGL-1 binds to CED-9 at the mitochondrial membrane to cause t...

    W D Fairlie, M A Perugini, M Kvansakul, L Chen, D C S Huang in Cell Death & Differentiation (2006)

  4. Article

    Modified vaccinia virus Ankara protein F1L is a novel BH3-domain-binding protein and acts together with the early viral protein E3L to block virus-associated apoptosis

    Infection with viruses often protects the infected cell against external stimuli to apoptosis. Here we explore the balance of apoptosis induction and inhibition for infection with the modified vaccinia virus A...

    S F Fischer, H Ludwig, J Holzapfel, M Kvansakul, L Chen in Cell Death & Differentiation (2006)