Thrombospondin (TSP) 2 is a close relative of TSP1 but differs in its temporal and spatial
distribution in the mouse. This difference in expression undoubtedly reflects the marked …

Using the cytoplasmic domain of Fas in the yeast twohybrid system, we have identified a
novel interacting protein, FADD, which binds Fasand Fas-FD5, a mutant of Fas possessing …

To identify CAP3 and CAP4, components of the CD95 (Fas/APO-1) death-inducing signaling
complex, we utilized nano-electrospray tandem mass spectrometry, a recently developed …

Although the mechanism of mammalian apoptosis has not been elucidated, a protease of
the CED-3/ICE family is anticipated to be a component of the death machinery. Several lines …

R current appreciation of the involvement of hrombospondin 1 (TSP1) 1 in diverse biological
processes (Fig. 1; 1, 3, 25) extends far beyond the role initially attributed to the protein in …

Subunit oligomerization of many proteins is mediated by α-helical coiled-coil domains. 3, 4-
Hydrophobic heptad repeat sequences, the characteristic feature of the coiled-coil protein …

THE effector arm of the cell-death pathway is composed of cysteine proteases belonging to
the ICE/CED-3 family1, 2. In metazoan cells these exist as inactive polypeptide precursors …

Rat bone marrow stromal cells comprise a heterogeneous mixture of cell lineages including
osteoblastic cells. When grown in the presence of ascorbic acid, β-glycerophosphate and …

ProIL-1β is a proinflammatory cytokine that is proteolytically processed to its active form by
caspase-1. Upon receipt of a proinflammatory stimulus, an upstream adaptor, RIP2, binds …

Molluscum contagiosum virus proteins MC159 and MC160 and the equine herpesvirus 2
protein E8 share substantial homology to the death effector domain present in the adaptor …