Zobrazeno 1 - 10
of 14
pro vyhledávání: '"Farhat Osman"'
Publikováno v:
Cell Reports, Vol 20, Iss 1, Pp 188-200 (2017)
Tumor necrosis factor alpha (TNF-α) is expressed promptly during inflammatory responses. Efficient TNF-α mRNA splicing is achieved through a 3′ UTR element that activates RNA-dependent eIF2α protein kinase (PKR). The TNF-α RNA activator, we sho
Externí odkaz:
https://doaj.org/article/b08a0644fc3049c88278087c2467dabc
Autor:
Raymond Kaempfer, Lena Ilan, Smadar Cohen-Chalamish, Orli Turgeman, Lise Sarah Namer, Farhat Osman
Publikováno v:
Frontiers in Genetics, Vol 10 (2019)
A critical step in the cellular stress response is transient activation of the RNA-dependent protein kinase PKR by double-helical RNA, resulting in down-regulation of protein synthesis through phosphorylation of the α chain of translation initiation
Externí odkaz:
https://doaj.org/article/64d3508dcf124420accf8e6bb274fa61
Autor:
Farhat Osman, Lena Ilan, Lise Sarah Namer, Einav Eliahu, Smadar Cohen-Chalamish, Raymond Kaempfer, Yona Banai, Yitzhak Ben-Asouli
Publikováno v:
Cell Research. 27:688-704
Short elements in mammalian mRNA can control gene expression by activating the RNA-dependent protein kinase PKR that attenuates translation by phosphorylating cytoplasmic eukaryotic initiation factor 2α (eIF2α). We demonstrate a novel, positive rol
Autor:
Lise Sarah Namer, Lena Ilan, Raymond Kaempfer, Orli Turgeman, Farhat Osman, Smadar Cohen-Chalamish
Publikováno v:
Frontiers in Genetics, Vol 10 (2019)
Frontiers in Genetics
Frontiers in Genetics
A critical step in the cellular stress response is transient activation of the RNA-dependent protein kinase PKR by double-helical RNA, resulting in down-regulation of protein synthesis through phosphorylation of the α chain of translation initiation
Publikováno v:
The international journal of biochemistrycell biology. 105
Once activated by double-helical RNA, mammalian RNA-dependent stress protein kinase, PKR, phosphorylates its substrate, translation initiation factor eIF2α, to inhibit translation. eIF2α phosphorylation is critical for mounting a cellular stress re
Autor:
Emmanuelle Supper, Ziv Rotfogel, Dalia Hillman, Revital Levy, Farhat Osman, Gila Arad, Andrey Popugailo, Raymond Kaempfer
Publikováno v:
Proceedings of the National Academy of Sciences. 113
Full T-cell activation requires interaction between the costimulatory receptors B7-2 and CD28. By binding CD28, bacterial superantigens elicit harmful inflammatory cytokine overexpression through an unknown mechanism. We show that, by engaging not on
Autor:
Raymond Kaempfer, Mark Katzenellenbogen, Elimelech Deutsch, Gila Arad, Farhat Osman, Doron J. Aframian, Mali Ketzinel, D. Sayar
Publikováno v:
Immunology Letters. 54:171-176
Human TNF-beta (lymphotoxin) gene expression is down-regulated by immunosuppression. Induction of TNF-beta mRNA in lymphoid cells is greatly enhanced by gamma-irradiation, cyclophosphamide and cimetidine, agents that each inhibit activation of suppre
Publikováno v:
Molecular and Cellular Biology. 16:2814-2822
2-Aminopurine (2-AP) inhibits specific kinases that phosphorylate the alpha subunit of eukaryotic translation initiation factor 2. One of these, PKR, is also involved in signal transduction. We show here that 2-AP selectively inhibits expression of t
Dynamic refolding of IFN-gamma mRNA enables it to function as PKR activator and translation template
Autor:
Dahlia Weinberg, Lise Sarah Namer, Anat Hasson, Yona Banai, Farhat Osman, Smadar Cohen-Chalamish, Raymond Kaempfer
Publikováno v:
Nature chemical biology. 5(12)
Interferon-gamma mRNA activates the RNA-dependent protein kinase PKR, which in turn strongly attenuates translation of interferon-gamma mRNA. Unlike riboswitches restricted to noncoding regions, the interferon-gamma RNA domain that activates PKR comp
Publikováno v:
Genesdevelopment. 13(24)
We report a role for the 3'-untranslated region in control of mRNA splicing and show that human TNF-alpha 3' UTR harbors a cis-acting element that renders splicing of precursor transcripts dependent on activation of PKR, the RNA-activated protein kin