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Soluble tumor necrosis factor (TNF) receptors are effective therapeutic agents in lethal endotoxemia and function simultaneously as both TNF carriers and TNF antagonists.
Results indicate that dimeric sTNFR are effective inhibitors of TNF and under some circumstances function simultaneously as both TNF "carriers" and antagonists of T NF biologic activity.
X-ray structures of the myosin motor domain of Dictyostelium discoideum complexed with MgADP.BeFx and MgADP.AlF4-.
The three-dimensional structures of the truncated myosin head from Dictyostelium discoideum myOSin II complexed with beryllium and aluminum fluoride and magnesium ADP are reported, indicating that myos in undergoes a conformational change during hydrolysis that is not associated with the nucleotide binding pocket but rather occurs in the COOH-terminal segment of the myosIn motor domain.
A receptor for tumor necrosis factor defines an unusual family of cellular and viral proteins.
The predicted cysteine-rich extracellular domain has extensive sequence similarity with five proteins, including nerve growth factor receptor and a transcriptionally active open reading frame from Shope fibroma virus, and thus defines a family of receptors.
Mechanism of antigen-driven selection in germinal centres
It is found that, on culture, centrocytes isolated from human tonsil kill themselves within a few hours by apoptosis, not a feature of other tonsillar B cells.
Fas ligand mediates activation-induced cell death in human T lymphocytes
The data indicate AICD in previously stimulated T cells is mediated by Fas/Fas-L interactions, and Fas-L antagonists inhibition of T cell clones and staphylococcus enterotoxin B (SEB)-specific T cell lines is indicated.
Apoptosis: molecular regulation of cell death.
Although apoptosis is now accepted as a critical element in the repertoire of potential cellular responses, the picture of the intra-cellular processes involved is probably still incomplete, not just in its details, but also in the basic outline of the process as a whole.
Structure of the MDM2/MDMX RING domain heterodimer reveals dimerization is required for their ubiquitylation in trans
The crystal structure of the MDM2/MDMX RING domain heterodimer and map residues required for functional interaction with the E2 are reported and it is shown that these residues are part of an extended surface that is essential for ubiquitylation in trans.