Structure–activity relationship of the p55 TNF receptor death domain and its lymphoproliferation mutants

Upon stimulation with tumor necrosis factor (TNF), the TNF receptor (TNFR55) mediates a multitude of effects both in normal and in tumor cells. Clustering of the intracellular domain of the receptor, the so‐called death domain (DD), is responsible for both the initiation of cell killing and the acti...

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Veröffentlicht in:	European journal of biochemistry 2001-03, Vol.268 (5), p.1382-1391
Hauptverfasser:	De Wilde, Gert, Murray‐Rust, Judith, Boone, Elke, Olerenshaw, Dionne, McDonald, Neil Q., Ibanez, Carlos, Haegeman, Guy, Wollmer, Axel, Federwisch, Matthias
Format:	Artikel
Sprache:	eng
Schlagworte:	Adaptor Proteins, Signal Transducing Amino Acid Sequence Animals Antigens, CD - chemistry Antigens, CD - genetics Antigens, CD - metabolism Carrier Proteins - chemistry Circular Dichroism Escherichia coli fas Receptor - chemistry Fas-Associated Death Domain Protein fluorescence spectroscopy Guanidine - pharmacology homology modeling Humans Medicin och hälsovetenskap Mice Models, Molecular Molecular Sequence Data Mutation - genetics Phenotype Protein Denaturation - drug effects Protein Structure, Secondary Protein Structure, Tertiary Receptor, Nerve Growth Factor - chemistry Receptors, Tumor Necrosis Factor - chemistry Receptors, Tumor Necrosis Factor - genetics Receptors, Tumor Necrosis Factor - metabolism Receptors, Tumor Necrosis Factor, Type I Recombinant Fusion Proteins - chemistry Recombinant Fusion Proteins - metabolism Sequence Alignment Signal Transduction Spectrometry, Fluorescence stability Structure-Activity Relationship Thioredoxins - chemistry Thioredoxins - genetics Thioredoxins - metabolism Tumor Cells, Cultured
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