About: Nuclear proteins hijacked by mammalian cytoplasmic plus strand RNA viruses

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An Entity of Type : schema:ScholarlyArticle, within Data Space : covidontheweb.inria.fr associated with source document(s)

Attributes	Values
type	Academic Article research paper schema:ScholarlyArticle
isDefinedBy	Covid-on-the-Web dataset
has title	Nuclear proteins hijacked by mammalian cytoplasmic plus strand RNA viruses
Creator	Lloyd, Richard
Source	Elsevier; Medline; PMC
abstract	Abstract Plus strand RNA viruses that replicate in the cytoplasm face challenges in supporting the numerous biosynthetic functions required for replication and propagation. Most of these viruses are genetically simple and rely heavily on co-opting cellular proteins, particularly cellular RNA-binding proteins, into new roles for support of virus infection at the level of virus-specific translation, and building RNA replication complexes. In the course of infectious cycles many nuclear-cytoplasmic shuttling proteins of mostly nuclear distribution are detained in the cytoplasm by viruses and re-purposed for their own gain. Many mammalian viruses hijack a common group of the same factors. This review summarizes recent gains in our knowledge of how cytoplasmic RNA viruses use these co-opted host nuclear factors in new functional roles supporting virus translation and virus RNA replication and common themes employed between different virus groups.
has issue date	2015-05-31(xsd:dateTime)
bibo:doi	10.1016/j.virol.2015.03.001
bibo:pmid	25818028
has license	els-covid
sha1sum (hex)	601e93e5f13dc9a322c1bfd6170f0f76d0949c65
schema:url	https://doi.org/10.1016/j.virol.2015.03.001
resource representing a document's title	Nuclear proteins hijacked by mammalian cytoplasmic plus strand RNA viruses
has PubMed Central identifier	PMC4426963
has PubMed identifier	25818028
schema:publication	Virology
resource representing a document's body	covid:601e93e5f13dc9a322c1bfd6170f0f76d0949c65#body_text
is schema:about of	named entity 'viruses' named entity 'MAMMALIAN' named entity 'NUCLEAR PROTEINS' named entity 'RNA VIRUSES' named entity 'CYTOPLASMIC' named entity 'Picornavirus' named entity 'RNA replication' named entity 'ns5B' named entity 'cis' named entity 'protein' named entity 'nuclear proteins' named entity 'innate immune' named entity 'viral RNA replication' named entity 'genome' named entity 'viral RNA' named entity 'genome' named entity 'isoform' named entity 'virus replication' named entity 'binding motif' named entity 'stress granules' named entity 'infection' named entity 'Blyn' named entity 'RNA' named entity 'cytoplasmic' named entity 'RHA' named entity 'UTRs' named entity 'poliovirus' named entity 'ribosomes' named entity 'RNA synthesis' named entity 'DENV' named entity 'UTR' named entity 'UTRs' named entity 'DENV' named entity 'cleavage' named entity 'HCV' named entity 'IRES' named entity 'PCBP1' named entity 'mRNA' named entity 'nuclear factor' named entity 'translation initiation' named entity 'ITAF' named entity 'nucleating' named entity 'HCV' named entity 'SRp20' named entity 'IRESs' named entity 'replicon' named entity 'Piñeiro' named entity 'IRES' named entity 'RNA-binding' named entity 'C-terminal' named entity 'IRES' named entity 'PCBP2' named entity 'mouse hepatitis virus' named entity 'proteomics' named entity 'nucleolin' named entity 'cyclization' named entity 'poliovirus' named entity 'RNA-binding proteins' named entity 'Sindbis virus' named entity 'Gemin5' named entity 'wild type' named entity 'HCV' named entity 'IRES' named entity 'Japanese Encephalitis virus' named entity 'HCV' named entity 'hnRNP A1' named entity 'click chemistry' named entity 'proteomics' named entity 'RNA synthesis' named entity 'feline calicivirus' named entity 'nucleolin' named entity 'cytoplasmic' named entity 'hnRNP A1' named entity 'hnRNP C' named entity 'ribosome' named entity 'cytoplasm' named entity 'murine norovirus' named entity 'Type 1' named entity 'RNA' named entity 'poliovirus' named entity 'cytoplasmic'

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