scholarly journals Azadirachtin interacts with the tumor necrosis factor (TNF) binding domain of its receptors and inhibits TNF-induced biological responses.

2012 ◽  
Vol 287 (17) ◽  
pp. 13556-13556
Author(s):  
Maikho Thoh ◽  
Pankaj Kumar ◽  
Hampathalu A. Nagarajaram ◽  
Sunil K. Manna
Keyword(s):  
Tumor Necrosis Factor ◽  
Tumor Necrosis ◽  
Binding Domain ◽  
Biological Responses ◽  
Necrosis Factor

scholarly journals A chemokine-binding domain in the tumor necrosis factor receptor from variola (smallpox) virus

2006 ◽  
Vol 103 (15) ◽  
pp. 5995-6000 ◽  
Author(s):  
A. Alejo ◽  
M. B. Ruiz-Arguello ◽  
Y. Ho ◽  
V. P. Smith ◽  
M. Saraiva ◽  
...  
Keyword(s):  
Tumor Necrosis Factor ◽  
Tumor Necrosis ◽  
Tumor Necrosis Factor Receptor ◽  
Binding Domain ◽  
Smallpox Virus ◽  
Necrosis Factor

scholarly journals BAFF, a Novel Ligand of the Tumor Necrosis Factor Family, Stimulates B Cell Growth

1999 ◽  
Vol 189 (11) ◽  
pp. 1747-1756 ◽  
Author(s):  
Pascal Schneider ◽  
Fabienne MacKay ◽  
Véronique Steiner ◽  
Kay Hofmann ◽  
Jean-Luc Bodmer ◽  
...  
Keyword(s):  
B Cells ◽  
Cell Growth ◽  
Tumor Necrosis Factor ◽  
B Cell ◽  
Tumor Necrosis ◽  
Immunoglobulin M ◽  
Biological Responses ◽  
Membrane Bound ◽  
And Function ◽  
Necrosis Factor

Members of the tumor necrosis factor (TNF) family induce pleiotropic biological responses, including cell growth, differentiation, and even death. Here we describe a novel member of the TNF family, designated BAFF (for B cell activating factor belonging to the TNF family), which is expressed by T cells and dendritic cells. Human BAFF was mapped to chromosome 13q32-34. Membrane-bound BAFF was processed and secreted through the action of a protease whose specificity matches that of the furin family of proprotein convertases. The expression of BAFF receptor appeared to be restricted to B cells. Both membrane-bound and soluble BAFF induced proliferation of anti-immunoglobulin M–stimulated peripheral blood B lymphocytes. Moreover, increased amounts of immunoglobulins were found in supernatants of germinal center–like B cells costimulated with BAFF. These results suggest that BAFF plays an important role as costimulator of B cell proliferation and function.

scholarly journals Dimerization of the IκB Kinase-Binding Domain of NEMO Is Required for Tumor Necrosis Factor Alpha-Induced NF-κB Activity

2006 ◽  
Vol 26 (24) ◽  
pp. 9209-9219 ◽  
Author(s):  
Ralf B. Marienfeld ◽  
Lysann Palkowitsch ◽  
Sankar Ghosh
Keyword(s):  
Tumor Necrosis Factor ◽  
Tumor Necrosis ◽  
Binding Domain ◽  
Amino Terminus ◽  
Necrosis Factor Alpha ◽  
Amino Terminal ◽  
Iκb Kinase ◽  
Ikk Complex ◽  
Factor Alpha ◽  
Necrosis Factor

ABSTRACT Previous studies have demonstrated that peptides corresponding to a six-amino-acid NEMO-binding domain from the C terminus of IκB kinase alpha (IKKα) and IKKβ can disrupt the IKK complex and block NF-κB activation. We have now mapped and characterized the corresponding amino-terminal IKK-binding domain (IBD) of NEMO. Peptides corresponding to the IBD were efficiently recruited to the IKK complex but displayed only a weak inhibitory potential on cytokine-induced NF-κB activity. This is most likely due to the formation of sodium dodecyl sulfate- and urea-resistant NEMO dimers through a dimerization domain at the amino terminus of NEMO that overlaps with the region responsible for binding to IKKs. Mutational analysis revealed different α-helical subdomains within an amino-terminal coiled-coil region are important for NEMO dimerization and IKKβ binding. Furthermore, NEMO dimerization is required for the tumor necrosis factor alpha-induced NF-κB activation, even when interaction with the IKKs is unaffected. Hence, our data provide novel insights into the role of the amino terminus of NEMO for the architecture of the IKK complex and its activation.

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