Zobrazeno 1 - 10
of 40
pro vyhledávání: '"Lee Heston"'
Publikováno v:
PLoS ONE, Vol 10, Iss 5, p e0126088 (2015)
Epstein Barr virus (EBV), like other oncogenic viruses, modulates the activity of cellular DNA damage responses (DDR) during its life cycle. Our aim was to characterize the role of early lytic proteins and viral lytic DNA replication in activation of
Externí odkaz:
https://doaj.org/article/f4b6489203704dbaaf501efd9b195439
Autor:
Richard Park, Ayman El-Guindy, Lee Heston, Su-Fang Lin, Kuan-Ping Yu, Mate Nagy, Sumit Borah, Henri-Jacques Delecluse, Joan Steitz, George Miller
Publikováno v:
PLoS ONE, Vol 9, Iss 4, p e92593 (2014)
Many viruses target cytoplasmic polyA binding protein (PABPC) to effect widespread inhibition of host gene expression, a process termed viral host-shutoff (vhs). During lytic replication of Epstein Barr Virus (EBV) we observed that PABPC was efficien
Externí odkaz:
https://doaj.org/article/b66814ce22764b37b04800f3aeaea430
Publikováno v:
PLoS Pathogens, Vol 6, Iss 8, p e1001054 (2010)
ZEBRA is a site-specific DNA binding protein that functions as a transcriptional activator and as an origin binding protein. Both activities require that ZEBRA recognizes DNA motifs that are scattered along the viral genome. The mechanism by which ZE
Externí odkaz:
https://doaj.org/article/4f644a04f3a846db8e434f8df5adb233
Autor:
Erin Weber, Yong Xiong, George Miller, Lee Heston, Olga Buzovetsky, Ayman El-Guindy, Kirsten M. Knecht, Kuan-Ping Yu
Publikováno v:
Journal of Virology
The pathogenesis of Epstein-Barr virus (EBV) infection, including development of lymphomas and carcinomas, is dependent on the ability of the virus to transit from latency to the lytic phase. This conversion, and ultimately disease development, depen
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b308923796953487dd59bf9529d49098
https://europepmc.org/articles/PMC6600195/
https://europepmc.org/articles/PMC6600195/
Autor:
Dirk P. Dittmer, Danielle E. Lyons, Lee Heston, Kuan-Ping Yu, Ayman El-Guindy, Jason A. Vander Heiden, George Miller
Publikováno v:
Journal of Virology. 92
Epstein-Barr virus (EBV) ZEBRA protein activates the EBV lytic cycle. Cellular AP-1 proteins with alanine-to-serine [AP-1(A/S)] substitutions homologous to ZEBRA(S186) assume some functions of EBV ZEBRA. These AP-1(A/S) mutants bind methylated EBV DN
Autor:
Zhaowei Ding, Ruth Wang'ondu, Lee Heston, Kuan Ping Yu, George Miller, Henri Jacques Delecluse, Richard Park
Publikováno v:
Proceedings of the National Academy of Sciences. 110:8176-8181
ZEBReplication Activator (ZEBRA), a viral basic zipper protein that initiates the Epstein–Barr viral lytic cycle, binds to DNA and activates transcription through heptamer ZEBRA response elements (ZREs) related to AP-1 sites. A component of the bio
Publikováno v:
Journal of Biological Chemistry. 286:9748-9762
Nuclear aggresomes induced by proteins containing an expanded polyglutamine (polyQ) tract are pathologic hallmarks of certain neurodegenerative diseases. Some GFP fusion proteins lacking a polyQ tract may also induce nuclear aggresomes in cultured ce
Autor:
L Gradoville, J. Countryman, Lee Heston, George Miller, Jianjiang Ye, Sarah Himmelfarb, Sumita Bhaduri-McIntosh, Duane Shedd
Publikováno v:
Journal of Virology. 83:10694-10709
Epstein-Barr virus (EBV) can be reactivated from latency into the lytic cycle by many stimuli believed to operate by different mechanisms. Cell lines containing EBV differ in their responses to inducing stimuli, yet all stimuli require de novo protei
Publikováno v:
Journal of Virology. 81:3303-3316
The Epstein-Barr virus ZEBRA protein controls the viral lytic cycle. ZEBRA activates the transcription of viral genes required for replication. ZEBRA also binds to oriLyt and interacts with components of the viral replication machinery. The mechanism
Publikováno v:
Journal of Virology. 76:11199-11208
ZEBRA protein converts Epstein-Barr virus (EBV) infection from the latent to the lytic state. The ability of ZEBRA to activate this switch is strictly dependent on the presence of serine or threonine at residue 186 of the protein (A. Francis, T. Rago