Temperature-sensitive lesions in two influenza A viruses defective for replicative transcription disrupt RNA binding by the nucleoprotein.
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Cyclophilin E functions as a negative regulator to influenza virus replication by impairing the formation of the viral ribonucleoprotein complexDefinition of the minimal viral components required for the initiation of unprimed RNA synthesis by influenza virus RNA polymeraseFunctional analysis of PA binding by influenza a virus PB1: effects on polymerase activity and viral infectivityModel suggesting that replication of influenza virus is regulated by stabilization of replicative intermediatesAn inhibitory activity in human cells restricts the function of an avian-like influenza virus polymerase.A big role for small RNAs in influenza virus replicationIdentification of BPR3P0128 as an inhibitor of cap-snatching activities of influenza virus.Influenza A virus expresses high levels of an unusual class of small viral leader RNAs in infected cellsStructural and functional characterization of an influenza virus RNA polymerase-genomic RNA complexInfluenza polymerase activity correlates with the strength of interaction between nucleoprotein and PB2 through the host-specific residue K/E627.RNA interference of influenza virus production by directly targeting mRNA for degradation and indirectly inhibiting all viral RNA transcriptionTemperature sensitive influenza A virus genome replication results from low thermal stability of polymerase-cRNA complexes.Replication-coupled and host factor-mediated encapsidation of the influenza virus genome by viral nucleoprotein.Structural characterization of the viral and cRNA panhandle motifs from the infectious salmon anemia virus.Modeling the intracellular dynamics of influenza virus replication to understand the control of viral RNA synthesis.Structure of influenza virus ribonucleoprotein complexes and their packaging into virions.The influenza virus RNA synthesis machine: advances in its structure and function.Influenza A Virus Nucleoprotein: A Highly Conserved Multi-Functional Viral Protein as a Hot Antiviral Drug Target.Identification of amino acid residues of influenza virus nucleoprotein essential for RNA binding.Interaction of the influenza virus nucleoprotein with the cellular CRM1-mediated nuclear export pathwayFunctional analysis of the influenza virus H5N1 nucleoprotein tail loop reveals amino acids that are crucial for oligomerization and ribonucleoprotein activities.De novo replication of the influenza virus RNA genome is regulated by DNA replicative helicase, MCM.The PA subunit is required for efficient nuclear accumulation of the PB1 subunit of the influenza A virus RNA polymerase complex.Role of initiating nucleoside triphosphate concentrations in the regulation of influenza virus replication and transcription.Nuclear dynamics of influenza A virus ribonucleoproteins revealed by live-cell imaging studies.Studies of an influenza A virus temperature-sensitive mutant identify a late role for NP in the formation of infectious virionsIdentification of the domains of the influenza A virus M1 matrix protein required for NP binding, oligomerization and incorporation into virions.Differential polymerase activity in avian and mammalian cells determines host range of influenza virus.Influenza virion-derived viral ribonucleoproteins synthesize both mRNA and cRNA in vitro.The role and assembly mechanism of nucleoprotein in influenza A virus ribonucleoprotein complexes.
P2860
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P2860
Temperature-sensitive lesions in two influenza A viruses defective for replicative transcription disrupt RNA binding by the nucleoprotein.
description
1999 nî lūn-bûn
@nan
1999年の論文
@ja
1999年論文
@yue
1999年論文
@zh-hant
1999年論文
@zh-hk
1999年論文
@zh-mo
1999年論文
@zh-tw
1999年论文
@wuu
1999年论文
@zh
1999年论文
@zh-cn
name
Temperature-sensitive lesions ...... binding by the nucleoprotein.
@en
Temperature-sensitive lesions ...... binding by the nucleoprotein.
@nl
type
label
Temperature-sensitive lesions ...... binding by the nucleoprotein.
@en
Temperature-sensitive lesions ...... binding by the nucleoprotein.
@nl
prefLabel
Temperature-sensitive lesions ...... binding by the nucleoprotein.
@en
Temperature-sensitive lesions ...... binding by the nucleoprotein.
@nl
P2093
P2860
P1433
P1476
Temperature-sensitive lesions ...... binding by the nucleoprotein.
@en
P2093
P2860
P304
P407
P577
1999-09-01T00:00:00Z