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

• Published in: Journal of Virology Vol. 68; no. 7; pp. 4137 - 4151
• Main Authors: Ghadge, G D, Malhotra, P, Furtado, M R, Dhar, R, Thimmapaya, B
• Format: Journal Article
• Language: English
• Published: Washington, DC American Society for Microbiology 01.07.1994
• Subjects: adenovirus; Adenoviruses, Human - genetics; Base Sequence; Biological and medical sciences; eIF-2 Kinase; Enzyme Activation; Fundamental and applied biological sciences. Psychology; Genetics; HeLa Cells; Humans; Microbiology; Molecular Sequence Data; Mutation; Nucleic Acid Conformation; Phenotype; Phosphorylation; Protein-Serine-Threonine Kinases - antagonists & inhibitors; Protein-Serine-Threonine Kinases - metabolism; RNA, Double-Stranded - metabolism; RNA, Viral - chemistry; RNA, Viral - genetics; RNA, Viral - metabolism; Virology; Hairpin loop; Adenoviridae; Nucleotide sequence; Enzyme; Transferases; Molecular interaction; Secondary structure; Host virus relation; In vitro; Structure function relationship; Virus; Protein kinase; Mutation; Structural analysis
• ISSN: 0022-538X; 1098-5514
• DOI: 10.1128/JVI.68.7.4137-4151.1994

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