Zobrazeno 1 - 10
of 77
pro vyhledávání: '"Elliott Kieff"'
Autor:
Tyler Colson, Elliott Kieff, Stefanie C.S. Schmidt, Shuangqi Wang, Benjamin E. Gewurz, Sizun Jiang, Bo Zhao, Liangru Ke, Catherine Gerdt, Yijie Ma, Chong Wang, Yohei Narita, Jun Liang, Guoliang Li, Hufeng Zhou
Epstein-Barr virus (EBV) transforms B cells to continuously proliferating lymphoblastoid cell lines (LCLs), which represent an experimental model for EBV-associated cancers. EBV nuclear antigens (EBNAs) and LMP1 are EBV transcriptional regulators tha
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1ba27a2f324a12dbb6d19ca98b51d11b
https://europepmc.org/articles/PMC5662195/
https://europepmc.org/articles/PMC5662195/
Publikováno v:
Cellular Signalling. 26:2730-2737
TRAFs constitute a family of proteins that have been implicated in signal transduction by immunomodulatory cellular receptors and viral proteins. TRAF2 and TRAF6 have an E3-ubiquitin ligase activity, which is dependent on the integrity of their RING
Autor:
Edward Bedoya, Elliott Kieff, John Quackenbush, Kaoru Takasaki, Jessica C. Mar, James Y. Zou, Megha Padi, Benjamin E. Gewurz, Bo Zhao, Ellen Cahir-McFarland, Nicholas P. Shinners
Publikováno v:
Journal of Virology. 85:6764-6773
Epstein-Barr virus (EBV) latent membrane protein 1 (LMP1) transforms rodent fibroblasts and is expressed in most EBV-associated malignancies. LMP1 ( t ransformation e ffector s ite 2 [TES2]/C-terminal activation region 2 [CTAR2]) activates NF-κB, p3
Autor:
Daisuke Okuzaki, Chiau-Yuang Tsai, Shuhei Sakakibara, Yijie Ma, Takeharu Minamitani, Hitoshi Kikutani, Benjamin E. Gewurz, Teruhito Yasui, Hufeng Zhou, Elliott Kieff
Epstein-Barr virus (EBV) infects germinal center (GC) B cells and establishes persistent infection in memory B cells. EBV-infected B cells can cause B-cell malignancies in humans with T- or natural killer-cell deficiency. We now find that EBV-encoded
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::454cb6133209454e54c0c4b8656c0e88
https://europepmc.org/articles/PMC4577157/
https://europepmc.org/articles/PMC4577157/
Publikováno v:
Journal of Virology. 80:10787-10793
The Epstein-Barr virus oncoprotein LMP1 has six transmembrane domains (TMs) that enable intermolecular aggregation and constitutive signaling through two C-terminal cytosolic domains. Expression of both TMs 1 and 2 without the C terminus (TM1-2ΔC) a
Publikováno v:
Proceedings of the National Academy of Sciences. 103:2689-2694
Epstein-Barr virus latent infection integral membrane protein 1 (LMP1) mimics a constitutively active TNF receptor (TNFR). LMP1 has two C-terminal cytosolic domains, transformation effector sites (TES)1 and -2, that engage TNFR-associated factors (TR
Autor:
Micah A. Luftig, Teruhito Yasui, Vishal Soni, N. G. Jacobson, Brian Seed, Ellen Cahir-McFarland, Myung-Soo Kang, Elliott Kieff
Publikováno v:
Proceedings of the National Academy of Sciences. 101:141-146
Epstein-Barr virus (EBV) latent infection membrane protein 1 (LMP1)-induced NF-kappaB activation is important for infected cell survival. LMP1 activates NF-kappaB, in part, by engaging tumor necrosis factor (TNF) receptor-associated factors (TRAFs),
Publikováno v:
Molecular and cellular biology. 34(3)
We have previously reported that interleukin-1 (IL-1) receptor-associated kinase (IRAK1) is essential for Epstein-Barr virus (EBV) latent infection membrane protein 1 (LMP1)-induced p65/RelA serine 536 phosphorylation and NF-κB activation but not fo
Publikováno v:
Proceedings of the National Academy of Sciences. 97:430-435
The Epstein–Barr virus (EBV) nuclear protein 2 (EBNA2) and herpes simplex virion protein 16 (VP16) acidic domains that mediate transcriptional activation now are found to have affinity for p300, CBP, and PCAF histone acetyltransferases (HATs). Tran
Autor:
Elisabeth A. Riley, Kenneth M. Izumi, Yuzhi Chen, Ellen Cahir McFarland, Danielle Rizzo, Elliott Kieff
Publikováno v:
Journal of Virology. 73:9908-9916
Epstein-Barr virus (EBV) latent membrane protein 1 (LMP1) is essential for EBV-mediated transformation of primary B lymphocytes. LMP1 spontaneously aggregates in the plasma membrane and enables two transformation effector sites (TES1 and TES2) within