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Baltimore Highlands, MD, United States

Brennan-Laun S.E.,Marlene and Stewart Greenebaum Cancer Center and | Brennan-Laun S.E.,University of Maryland, Baltimore | Ezelle H.J.,Marlene and Stewart Greenebaum Cancer Center and | Ezelle H.J.,University of Maryland, Baltimore | And 5 more authors.
Journal of Interferon and Cytokine Research | Year: 2014

RNase-L is a mediator of type 1 interferon-induced antiviral activity that has diverse and critical cellular roles, including the regulation of cell proliferation, differentiation, senescence and apoptosis, tumorigenesis, and the control of the innate immune response. Although RNase-L was originally shown to mediate the endonucleolytic cleavage of both viral and ribosomal RNAs in response to infection, more recent evidence indicates that RNase-L also functions in the regulation of cellular mRNAs as an important mechanism by which it exerts its diverse biological functions. Despite this growing body of work, many questions remain regarding the roles of mRNAs as RNase-L substrates. This review will survey known and putative mRNA substrates of RNase-L, propose mechanisms by which it may selectively cleave these transcripts, and postulate future clinical applications. © 2014 Mary Ann Liebert Inc. Source

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