In vitro analysis of virus-associated RNA I (VAI RNA): inhibition of the double-stranded RNA-activated protein kinase PKR by VAI RNA mutants correlates with the in vivo phenotype and the structural integrity of the central domain.
about
Microarray analysis identifies interferon-inducible genes and Stat-1 as major transcriptional targets of human papillomavirus type 31.Dissection of the adenoviral VA RNAI central domain structure reveals minimum requirements for RNA-mediated inhibition of PKR.Characterization and mapping of the double-stranded regions involved in activation of PKR within a cellular RNA from 3T3-F442A cellsRegulation of herpes simplex virus gamma(1)34.5 expression and oncolysis of diffuse liver metastases by Myb34.5.Structural features of adenovirus 2 virus-associated RNA required for binding to the protein kinase DAI.Controlling activation of the RNA-dependent protein kinase by siRNAs using site-specific chemical modificationEffect of single-base substitutions in the central domain of virus-associated RNA I on its function.Structure, function, and evolution of adenovirus-associated RNA: a phylogenetic approach.High level of transgene expression in cell cultures and in the mouse by replication-incompetent adenoviruses harboring modified VAI genesThe gamma(1)34.5 protein of herpes simplex virus 1 complexes with protein phosphatase 1alpha to dephosphorylate the alpha subunit of the eukaryotic translation initiation factor 2 and preclude the shutoff of protein synthesis by double-stranded RNA-Viral dsRNA inhibitors prevent self-association and autophosphorylation of PKR.Noncoding RNAs produced by oncogenic human herpesviruses.Adenovirus Vector-Derived VA-RNA-Mediated Innate Immune Responses.Domain interactions in adenovirus VAI RNA mediate high-affinity PKR binding.Systematic deletion of the adenovirus-associated RNAI terminal stem reveals a surprisingly active RNA inhibitor of double-stranded RNA-activated protein kinase.Characterization of the complete genome of the Tupaia (tree shrew) adenovirus.Analysis of adenovirus VA RNAI structure and stability using compensatory base pair modifications.Magnesium-dependent interaction of PKR with adenovirus VAI.The PKR-binding domain of adenovirus VA RNAI exists as a mixture of two functionally non-equivalent structures
P2860
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P2860
In vitro analysis of virus-associated RNA I (VAI RNA): inhibition of the double-stranded RNA-activated protein kinase PKR by VAI RNA mutants correlates with the in vivo phenotype and the structural integrity of the central domain.
description
1994 nî lūn-bûn
@nan
1994年の論文
@ja
1994年論文
@yue
1994年論文
@zh-hant
1994年論文
@zh-hk
1994年論文
@zh-mo
1994年論文
@zh-tw
1994年论文
@wuu
1994年论文
@zh
1994年论文
@zh-cn
name
In vitro analysis of virus-ass ...... tegrity of the central domain.
@ast
In vitro analysis of virus-ass ...... tegrity of the central domain.
@en
type
label
In vitro analysis of virus-ass ...... tegrity of the central domain.
@ast
In vitro analysis of virus-ass ...... tegrity of the central domain.
@en
prefLabel
In vitro analysis of virus-ass ...... tegrity of the central domain.
@ast
In vitro analysis of virus-ass ...... tegrity of the central domain.
@en
P2093
P2860
P1433
P1476
In vitro analysis of virus-ass ...... ntegrity of the central domain
@en
P2093
B Thimmapaya
G D Ghadge
M R Furtado
P Malhotra
P2860
P304
P407
P577
1994-07-01T00:00:00Z