Читать книгу Principles of Virology - Jane Flint, S. Jane Flint - Страница 298

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Structure of the hepatitis C virus RNA polymerase reveals that highly conserved active-site residues position the primer for attack on the incoming nucleotide.

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Structure of RNPs from virus particles reveals a double-helical conformation in which two strands of opposite polarity are associated along the helix.

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The use of electron tomography and image analysis reveals that isolate RNP filaments are not rigid helical structures.

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Structures of poliovirus RdRP reveal a pre-positioned templating base for nucleotide recognition, and a structural rearrangement in the palm domain leads to closure of catalytically active sites.

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Picornavirus RNA recombination counteracts the negative consequences of error-prone RNA replication.

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High-resolution structure reveals details of protein-protein and protein-RNA interactions.

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Structure of the L protein reveals a core RNA polymerase, an mRNA capping domain, and a methyltransferase domain.

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How the requirement for genome hexamer length, bipartite replication promoters, and P gene mRNA editing are linked among paramyxoviruses.

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Cryo-electron microscopy structure of influenza virus RNP reveals architecture and organization of the native complex.

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Crystal structure of trimeric influenza viral RdRP bound to its promoter, revealing mechanisms of activation and cap snatching.

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Structures of influenza virus RNA polymerase bound to viral RNA provide mechanistic insight into the different processes of mRNA synthesis and genome RNA replication.

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Identification of a tripartite polymerase complex associated with the viral proofreading enzyme.