Self-association of the “Death Domains” of the p55 Tumor Necrosis Factor (TNF) Receptor and Fas/APO1 Prompts Signaling for TNF and Fas/APO1 Effects
Open Access
- 1 January 1995
- journal article
- Published by Elsevier BV in Journal of Biological Chemistry
- Vol. 270 (1), 387-391
- https://doi.org/10.1074/jbc.270.1.387
Abstract
No abstract availableKeywords
This publication has 30 references indexed in Scilit:
- Screening for proteins that bind to the intracellular domains of the two tumor necrosis factor receptors (TNF-R) revealed effective self-association of the p55 TNF-R “death domain”, which can trigger signalingCytokine, 1994
- Molecular cloning and expression of the fas ligand, a novel member of the tumor necrosis factor familyCell, 1993
- A novel domain within the 55 kd TNF receptor signals cell deathCell, 1993
- A Receptor for Tumor Necrosis Factor Defines an Unusual Family of Cellular and Viral ProteinsScience, 1990
- Molecular cloning and expression of the human 55 kd tumor necrosis factor receptorCell, 1990
- Monoclonal Antibody-Mediated Tumor Regression by Induction of ApoptosisScience, 1989
- A novel genetic system to detect protein–protein interactionsNature, 1989
- A cell-killing monoclonal antibody (anti-Fas) to a cell surface antigen co-downregulated with the receptor of tumor necrosis factor.The Journal of Experimental Medicine, 1989
- Molecular cloning of a human monocyte-derived neutrophil chemotactic factor (MDNCF) and the induction of MDNCF mRNA by interleukin 1 and tumor necrosis factor.The Journal of Experimental Medicine, 1988
- Close similarity of epidermal growth factor receptor and v-erb-B oncogene protein sequencesNature, 1984