Comparison of the lipid-containing bacteriophages PRD1, PR3, PR4, PR5 and L17.
about
Genome annotation and intraviral interactome for the Streptococcus pneumoniae virulent phage Dp-1Maturation of IncP pilin precursors resembles the catalytic Dyad-like mechanism of leader peptidases.Viruses' life history: towards a mechanistic basis of a trade-off between survival and reproduction among phagesGIL16, a new gram-positive tectiviral phage related to the Bacillus thuringiensis GIL01 and the Bacillus cereus pBClin15 elementsThe VirB4 family of proposed traffic nucleoside triphosphatases: common motifs in plasmid RP4 TrbE are essential for conjugation and phage adsorptionPrimary structure of the DNA terminal protein of bacteriophage PRD1.In vitro replication of bacteriophage PRD1 DNA. Characterization of the protein-primed initiation site.Characterization of a DNA binding protein of bacteriophage PRD1 involved in DNA replication.In vitro replication of bacteriophage PRD1 DNA. Metal activation of protein-primed initiation and DNA elongation.Binding of an Escherichia coli double-stranded DNA virus PRD1 to a receptor coded by an IncP-type plasmidProtein-primed DNA replication: role of inverted terminal repeats in the Escherichia coli bacteriophage PRD1 life cycle.Methods for studying aquatic bacteriophage ecology.Identification of a protein bound to the termini of bacteriophage PRD1 DNA.Characterization of the DNA-protein complex at the termini of the bacteriophage PRD1 genomeIsolation of nonsense mutants of lipid-containing bacteriophage PRD1.Assembly of bacteriophage PRD1: particle formation with wild-type and mutant viruses.Structure of the lipid-containing bacteriophage PRD1: disruption of wild-type and nonsense mutant phage particles with guanidine hydrochloride.Stable packaging of phage PRD1 DNA requires adsorption protein P2, which binds to the IncP plasmid-encoded conjugative transfer complex.A new mutant class, made by targeted mutagenesis, of phage PRD1 reveals that protein P5 connects the receptor binding protein to the vertex.The lytic enzyme of bacteriophage PRD1 is associated with the viral membrane.The small viral membrane-associated protein P32 is involved in bacteriophage PRD1 DNA entryBacterial conjugation mediated by plasmid RP4: RSF1010 mobilization, donor-specific phage propagation, and pilus production require the same Tra2 core components of a proposed DNA transport complex.Changes in host cell energetics in response to bacteriophage PRD1 DNA entry.A specific protease encoded by the conjugative DNA transfer systems of IncP and Ti plasmids is essential for pilus synthesis.Functional organization of the bacteriophage PRD1 genome.DNA packaging orders the membrane of bacteriophage PRD1.Complete genome sequence of the broad host range single-stranded RNA phage PRR1 places it in the Levivirus genus with characteristics shared with Alloleviviruses.
P2860
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P2860
Comparison of the lipid-containing bacteriophages PRD1, PR3, PR4, PR5 and L17.
description
1981 nî lūn-bûn
@nan
1981年の論文
@ja
1981年論文
@yue
1981年論文
@zh-hant
1981年論文
@zh-hk
1981年論文
@zh-mo
1981年論文
@zh-tw
1981年论文
@wuu
1981年论文
@zh
1981年论文
@zh-cn
name
Comparison of the lipid-containing bacteriophages PRD1, PR3, PR4, PR5 and L17.
@en
type
label
Comparison of the lipid-containing bacteriophages PRD1, PR3, PR4, PR5 and L17.
@en
prefLabel
Comparison of the lipid-containing bacteriophages PRD1, PR3, PR4, PR5 and L17.
@en
P2093
P1476
Comparison of the lipid-containing bacteriophages PRD1, PR3, PR4, PR5 and L17.
@en
P2093
Bamford DH
Rouhiainen L
Söderlund H
Takkinen K
P304
P356
10.1099/0022-1317-57-2-365
P407
P577
1981-12-01T00:00:00Z