Literature DB >> 2471268

Double-stranded ribonuclease coinduced with interferon.

J M Meegan1, P I Marcus.   

Abstract

Double-stranded (ds) RNA and many viruses are inducers of interferon (IFN), the latter presumably because they contain, or can form, dsRNA. Concomitant with the induction of IFN in chicken embryo cells was the induction of a novel double-stranded ribonuclease (dsRNase), which was released into the medium and continued to accumulate long after IFN production ceased. Only avian cells (chicken, quail, turkey, or duck) expressed high levels of this dsRNase; mammalian, turtle, or fish cells did not. Production of the nuclease was inducer dose-dependent. Optimum pH and cation requirements distinguished it from other dsRNase activities. Degradation of dsRNA was endonucleolytic. Activity resided in a molecule of an Mr of approximately 34,500. Low levels of a single-stranded (ss) RNase activity were inseparable from the dsRNase. The role for a dsRNA-inducible dsRNase released from cells is unknown.

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Year:  1989        PMID: 2471268     DOI: 10.1126/science.2471268

Source DB:  PubMed          Journal:  Science        ISSN: 0036-8075            Impact factor:   47.728


  12 in total

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5.  Interferon induction and/or production and its suppression by influenza A viruses.

Authors:  Philip I Marcus; Jillian M Rojek; Margaret J Sekellick
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6.  cIRF-3, a new member of the interferon regulatory factor (IRF) family that is rapidly and transiently induced by dsRNA.

Authors:  C E Grant; M Z Vasa; R G Deeley
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Review 7.  Antisense RNA: function and fate of duplex RNA in cells of higher eukaryotes.

Authors:  M Kumar; G G Carmichael
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8.  Deletions at the C-terminus of interferon gamma reduce RNA binding and activation of double-stranded-RNA cleavage by bovine seminal ribonuclease.

Authors:  C H Schein; M Haugg
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9.  Revisiting the action of bovine ribonuclease A and pancreatic-type ribonucleases on double-stranded RNA.

Authors:  M Libonati; S Sorrentino
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10.  Defining the enzyme binding domain of a ribonuclease III processing signal. Ethylation interference and hydroxyl radical footprinting using catalytically inactive RNase III mutants.

Authors:  H Li; A W Nicholson
Journal:  EMBO J       Date:  1996-03-15       Impact factor: 11.598

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