Domain interactions in adenovirus VAI RNA mediate high-affinity PKR binding.
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Dissection of the adenoviral VA RNAI central domain structure reveals minimum requirements for RNA-mediated inhibition of PKR.Structural analysis of adenovirus VAI RNA defines the mechanism of inhibition of PKR.Identification of a gamma interferon-activated inhibitor of translation-like RNA motif at the 3' end of the transmissible gastroenteritis coronavirus genome modulating innate immune responseMicroRNAs as Important Players in Host-Adenovirus Interactions.
P2860
Domain interactions in adenovirus VAI RNA mediate high-affinity PKR binding.
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article científic
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article scientifique
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artigo científico
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bilimsel makale
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scientific article published on 04 January 2014
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vedecký článok
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Domain interactions in adenovirus VAI RNA mediate high-affinity PKR binding.
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Domain interactions in adenovirus VAI RNA mediate high-affinity PKR binding.
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Domain interactions in adenovirus VAI RNA mediate high-affinity PKR binding.
@en
Domain interactions in adenovirus VAI RNA mediate high-affinity PKR binding.
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Domain interactions in adenovirus VAI RNA mediate high-affinity PKR binding.
@en
Domain interactions in adenovirus VAI RNA mediate high-affinity PKR binding.
@nl
P2860
P1476
Domain interactions in adenovirus VAI RNA mediate high-affinity PKR binding.
@en
P2093
James L Cole
Katherine Launer-Felty
P2860
P304
P356
10.1016/J.JMB.2013.12.019
P407
P577
2014-01-04T00:00:00Z