Targeting of the influenza A virus polymerase PB1-PB2 interface indicates strain-specific assembly differences.
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The Influenza Virus Polymerase Complex: An Update on Its Structure, Functions, and Significance for Antiviral Drug DesignThe N-terminal fragment of a PB2 subunit from the influenza A virus (A/Hong Kong/156/1997 H5N1) effectively inhibits RNP activity and viral replicationComparative influenza protein interactomes identify the role of plakophilin 2 in virus restriction.Small molecule inhibitors of influenza A and B viruses that act by disrupting subunit interactions of the viral polymerase.Pandemic influenza A viruses escape from restriction by human MxA through adaptive mutations in the nucleoprotein.TRIM32 Senses and Restricts Influenza A Virus by Ubiquitination of PB1 PolymeraseStructure and assembly of the influenza A virus ribonucleoprotein complex.Adaptive mutations in NEP compensate for defective H5N1 RNA replication in cultured human cells.A peptide derived from the C-terminus of PB1 inhibits influenza virus replication by interfering with viral polymerase assembly.
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P2860
Targeting of the influenza A virus polymerase PB1-PB2 interface indicates strain-specific assembly differences.
description
2011 nî lūn-bûn
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2011年の論文
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2011年論文
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2011年論文
@zh-hant
2011年論文
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2011年論文
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2011年論文
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2011年论文
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2011年论文
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name
Targeting of the influenza A v ...... specific assembly differences.
@en
Targeting of the influenza A v ...... specific assembly differences.
@nl
type
label
Targeting of the influenza A v ...... specific assembly differences.
@en
Targeting of the influenza A v ...... specific assembly differences.
@nl
prefLabel
Targeting of the influenza A v ...... specific assembly differences.
@en
Targeting of the influenza A v ...... specific assembly differences.
@nl
P2093
P2860
P50
P356
P1433
P1476
Targeting of the influenza A v ...... specific assembly differences.
@en
P2093
Benjamin Mänz
Kerstin Wunderlich
Linda Brunotte
Peter Reuther
P2860
P304
13298-13309
P356
10.1128/JVI.00868-11
P407
P577
2011-09-28T00:00:00Z