Structural Requirements for Signal-induced Target Binding of FADD Determined by Functional Reconstitution of FADD Deficiency

This publication has 46 references indexed in Scilit:

• Identification of an Expanded Binding Surface on the FADD Death Domain Responsible for Interaction with CD95/Fas
  Journal of Biological Chemistry, 2004
• Cell Death
  Cell, 2004
• The three-dimensional solution structure and dynamic properties of the human FADD death domain 1 1Edited by A. Fersht
  Journal of Molecular Biology, 2000
• FLICE, A Novel FADD-Homologous ICE/CED-3–like Protease, Is Recruited to the CD95 (Fas/APO-1) Death-Inducing Signaling Complex
  Cell, 1996
• Involvement of MACH, a Novel MORT1/FADD-Interacting Protease, in Fas/APO-1- and TNF Receptor–Induced Cell Death
  Cell, 1996
• Targeted mutation in the Fas gene causes hyperplasia in peripheral lymphoid organs and liver
  Nature Genetics, 1995
• The death domain motif found in Fas (Apo‐1) and TNF receptor is present in proteins involved in apoptosis and axonal guidance
  FEBS Letters, 1995
• A novel domain within the 55 kd TNF receptor signals cell death
  Cell, 1993
• Lymphoproliferation disorder in mice explained by defects in Fas antigen that mediates apoptosis
  Nature, 1992
• Lpr and gld: Single Gene Models of Systemic Autoimmunity and Lymphoproliferative Disease
  Annual Review of Immunology, 1991