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Cited by 1,312

The DOI matches its Crossref record; 10 of the 10 references it cites were found in a registry or an index.

TUMOR NECROSIS FACTOR RECEPTOR AND Fas SIGNALING MECHANISMS

Wallach, D., Varfolomeev, E. E., Malinin, N. L., Goltsev, Yuri V., Kovalenko, A. V., Boldin, M. P.·1999·Annual Review of Immunology
DOI 10.1146/annurev.immunol.17.1.331
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Abstract

▪ Abstract Four members of the tumor necrosis factor (TNF) ligand family, TNF-α, LT-α, LT-β, and LIGHT, interact with four receptors of the TNF/nerve growth factor family, the p55 TNF receptor (CD120a), the p75 TNF receptor (CD120b), the lymphotoxin beta receptor (LTβR), and herpes virus entry mediator (HVEM) to control a wide range of innate and adaptive immune response functions. Of these, the most thoroughly studied are cell death induction and regulation of the inflammatory process. Fas/Apo1 (CD95), a receptor of the TNF receptor family activated by a distinct ligand, induces death in cells through mechanisms shared with CD120a. The last four years have seen a proliferation in knowledge of the proteins participating in the signaling by the TNF system and CD95. The downstream signaling molecules identified so far—caspases, phospholipases, the three known mitogen activated protein (MAP) kinase pathways, and the NF-κB activation cascade—mediate the effects of other inducers as well. However, the molecules that initiate these signaling events, including the death domain- and TNF receptor associated factor (TRAF) domain-containing adapter proteins and the signaling enzymes associated with them, are largely unique to the TNF/nerve growth factor receptor family.

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Crossref · 10.1146/annurev.immunol.17.1.331

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Metadata

Authors
Wallach, D., Varfolomeev, E. E., Malinin, N. L., Goltsev, Y. V., Kovalenko, A. V., & Boldin, M. P.
Venue
Annual Review of Immunology
Publisher
Annual Reviews
Published
1999-04
Volume
17
Issue
1
Pages
331-367
ISSN
  • 0732-0582 (ISSN-L)
  • 1545-3278
DOI
10.1146/annurev.immunol.17.1.331
OpenAlex
W2133726754
Cited by
1,312
References
10
FWCI
7.66
Type
journal article
Language
en
Open access
closed

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