In vitro replication, packaging, and transcription of the segmented double-stranded RNA genome of bacteriophage phi 6: studies with procapsids assembled from plasmid-encoded proteins.
about
Protein P7 of the cystovirus φ6 is located at the three-fold axis of the unexpanded procapsid.A mechanism for initiating RNA-dependent RNA polymerizationAdding the Third Dimension to Virus Life Cycles: Three-Dimensional Reconstruction of Icosahedral Viruses from Cryo-Electron MicrographsCharacterization of Phi2954, a newly isolated bacteriophage containing three dsRNA genomic segments.Three-dimensional structure of the enveloped bacteriophage phi12: an incomplete T = 13 lattice is superposed on an enclosed T = 1 shell.Precise packaging of the three genomic segments of the double-stranded-RNA bacteriophage phi6.Role of host protein glutaredoxin 3 in the control of transcription during bacteriophage Phi2954 infection.In vitro assembly of infectious nucleocapsids of bacteriophage phi 6: formation of a recombinant double-stranded RNA virus.Isolation and analysis of mutants of double-stranded-RNA bacteriophage phi6 with altered packaging specificity.The ϕ6 cystovirus protein P7 becomes accessible to antibodies in the transcribing nucleocapsid: a probe for viral structural elementsBacteriophage φ6--structure investigated by fluorescence Stokes shift spectroscopyDirected changes in the number of double-stranded RNA genomic segments in bacteriophage phi6.Stoichiometric packaging of the three genomic segments of double-stranded RNA bacteriophage phi6.Initial location of the RNA-dependent RNA polymerase in the bacteriophage Phi6 procapsid determined by cryo-electron microscopy.Template-dependent, in vitro replication of rotavirus RNA.Packaging motor from double-stranded RNA bacteriophage phi12 acts as an obligatory passive conduit during transcription.Reassortment in segmented RNA viruses: mechanisms and outcomes.Single-molecule measurements of viral ssRNA packaging.Mutational analysis of the role of nucleoside triphosphatase P4 in the assembly of the RNA polymerase complex of bacteriophage phi6.Nonspecific nucleoside triphosphatase P4 of double-stranded RNA bacteriophage phi6 is required for single-stranded RNA packaging and transcription.In vitro packaging of individual genomic segments of bacteriophage phi 6 RNA: serial dependence relationships.Interference with bacteriophage phi 6 genomic RNA packaging by hairpin structures.Double-stranded RNA bacteriophage phi 6 protein P4 is an unspecific nucleoside triphosphatase activated by calcium ions.Plasmid-directed assembly of the lipid-containing membrane of bacteriophage phi 6.Protein P4 of double-stranded RNA bacteriophage phi 6 is accessible on the nucleocapsid surface: epitope mapping and orientation of the protein.RNA structure and heterologous recombination in the double-stranded RNA bacteriophage phi 6.Construction of a transducing virus from double-stranded RNA bacteriophage phi6: establishment of carrier states in host cells.Expression of rotavirus VP2 produces empty corelike particles.Heterologous recombination in the double-stranded RNA bacteriophage phi 6.In vitro packaging and replication of individual genomic segments of bacteriophage phi 6 RNA.Dependence of minus-strand synthesis on complete genomic packaging in the double-stranded RNA bacteriophage phi 6.Protein P4 of the bacteriophage phi 6 procapsid has a nucleoside triphosphate-binding site with associated nucleoside triphosphate phosphohydrolase activity.What reassorts when reovirus genome segments reassort?Probing, by self-assembly, the number of potential binding sites for minor protein subunits in the procapsid of double-stranded RNA bacteriophage Φ6.The large genome segment of dsRNA bacteriophage phi6 is the key regulator in the in vitro minus and plus strand synthesis.Packaging and replication regulation revealed by chimeric genome segments of double-stranded RNA bacteriophage phi6.Rescue of maturation off-pathway products in the assembly of Pseudomonas phage φ 6A novel virus-host cell membrane interaction. Membrane voltage-dependent endocytic-like entry of bacteriophage straight phi6 nucleocapsid.RNA secondary structures of the bacteriophage phi6 packaging regions.Enzymatic mechanism of RNA translocation in double-stranded RNA bacteriophages.
P2860
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P2860
In vitro replication, packaging, and transcription of the segmented double-stranded RNA genome of bacteriophage phi 6: studies with procapsids assembled from plasmid-encoded proteins.
description
article científic
@ca
article scientifique
@fr
articolo scientifico
@it
artigo científico
@pt
bilimsel makale
@tr
scientific article published on October 1990
@en
vedecký článok
@sk
vetenskaplig artikel
@sv
videnskabelig artikel
@da
vědecký článek
@cs
name
In vitro replication, packagin ...... from plasmid-encoded proteins.
@en
In vitro replication, packagin ...... from plasmid-encoded proteins.
@nl
type
label
In vitro replication, packagin ...... from plasmid-encoded proteins.
@en
In vitro replication, packagin ...... from plasmid-encoded proteins.
@nl
prefLabel
In vitro replication, packagin ...... from plasmid-encoded proteins.
@en
In vitro replication, packagin ...... from plasmid-encoded proteins.
@nl
P2093
P2860
P1476
In vitro replication, packagin ...... from plasmid-encoded proteins.
@en
P2093
P2860
P304
P356
10.1128/JB.172.10.5774-5782.1990
P407
P577
1990-10-01T00:00:00Z