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Cited by 137

The DOI matches its Crossref record; 41 of the 41 references it cites were found in a registry or an index.

Epstein–Barr virus-transforming protein latent infection membrane protein 1 activates transcription factor NF-κB through a pathway that includes the NF-κB-inducing kinase and the IκB kinases IKKα and IKKβ

Sylla, Bakary S., Hung, Siu Chun, Davidson, David M., Hatzivassiliou, Eudoxia, Malinin, Nikolai L., Wallach, David, Gilmore, Thomas D., Kieff, Elliott, Mosialos, George·1998·Proceedings of the National Academy of Sciences

Abstract

The Epstein–Barr virus oncoprotein latent infection membrane protein 1 (LMP1) is a constitutively aggregated pseudo-tumor necrosis factor receptor (TNFR) that activates transcription factor NF-κB through two sites in its C-terminal cytoplasmic domain. One site is similar to activated TNFRII in associating with TNFR-associated factors TRAF1 and TRAF2, and the second site is similar to TNFRI in associating with the TNFRI death domain interacting protein TRADD. TNFRI has been recently shown to activate NF-κB through association with TRADD, RIP, and TRAF2; activation of the NF-κB-inducing kinase (NIK); activation of the IκBα kinases (IKKα and IKKβ); and phosphorylation of IκBα. IκBα phosphorylation on Ser-32 and Ser-36 is followed by its degradation and NF-κB activation. In this report, we show that NF-κB activation by LMP1 or by each of its effector sites is mediated by a pathway that includes NIK, IKKα, and IKKβ. Dominant negative mutants of NIK, IKKα, or IKKβ substantially inhibited NF-κB activation by LMP1 or by each of its effector sites.

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Crossref · 10.1073/pnas.95.17.10106

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Research works printed but not linked: 3

  1. E Kieff in Fields Virology, eds B N Fields, D M Knipe, P M Howley (Lippincott-Raven, Philadelphia), pp. 2343–2396 (1996).
  2. D S Huen, S A Henderson, C D Croom, M Rowe Oncogene 10, 549–560 (1995).
  3. V R Baichwal, B Sugden Oncogene 4, 67–74 (1989).

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Metadata

Authors
Sylla, B. S., Hung, S. C., Davidson, D. M., Hatzivassiliou, E., Malinin, N. L., Wallach, D., Gilmore, T. D., Kieff, E., & Mosialos, G.
Affiliations
Departments of Microbiology and Molecular Genetics and Medicine, Harvard Medical School and Brigham and Women’s Hospital, 181 Longwood Avenue, Boston, MA, 02115; Department of Membrane Research and Biophysics, The Weizmann Institute of Science, 76100 Rehovot, Israel; and Department of Biology, Boston University, 5 Cummington Street, Boston, MA 02215
Venue
Proceedings of the National Academy of Sciences
Published
1998-08-18
Volume
95
Issue
17
Pages
10106-10111
ISSN
  • 0027-8424
  • 1091-6490
Cited by
137
References
41
Language
en

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