Enforced covalent trimerization increases the activity of the TNF ligand family members TRAIL and CD95L-Reference-Cited by-同舟云学术

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Enforced covalent trimerization increases the activity of the TNF ligand family members TRAIL and CD95L

Published:2007-08-17 Issue:12 Volume:14 Page:2021-2034
ISSN:1350-9047
Container-title:Cell Death & Differentiation
language:en
Short-container-title:Cell Death Differ

Author:

Berg D,Lehne M,Müller N,Siegmund D,Münkel S,Sebald W,Pfizenmaier K,Wajant H

Publisher

Springer Science and Business Media LLC

Subject

Cell Biology,Molecular Biology

Link

http://www.nature.com/articles/4402213.pdf

Reference24 articles.

1. Locksley RM, Killeen N, Lenardo MJ . The TNF and TNF receptor superfamilies: integrating mammalian biology. Cell 2001; 104: 487–501.

2. Bodmer JL, Schneider P, Tschopp J . The molecular architecture of the TNF superfamily. Trends Biochem Sci 2002; 27: 19–26.

3. Grell M, Douni E, Wajant H, Lohden M, Clauss M, Maxeiner B et al. The transmembrane form of tumor necrosis factor is the prime activating ligand of the 80 kDa tumor necrosis factor receptor. Cell 1995; 83: 793–802.

4. Schneider P, Holler N, Bodmer JL, Hahne M, Frei K, Fontana A et al. Conversion of membrane-bound Fas(CD95) ligand to its soluble form is associated with downregulation of its proapoptotic activity and loss of liver toxicity. J Exp Med 1998; 187: 1205–1213.

5. Wajant H, Moosmayer D, Wuest T, Bartke T, Gerlach E, Schonherr U et al. Differential activation of TRAIL-R1 and -2 by soluble and membrane TRAIL allows selective surface antigen-directed activation of TRAIL-R2 by a soluble TRAIL derivative. Oncogene 2001; 20: 4101–4106.

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