Published in BMC Microbiol on August 23, 2011
Structural insight into the DNA-binding mode of the primosomal proteins PriA, PriB, and DnaT. Biomed Res Int (2014) 0.80
Deinococcus radiodurans PriA is a Pseudohelicase. PLoS One (2015) 0.75
The importance of repairing stalled replication forks. Nature (2000) 7.93
Replisome assembly and the direct restart of stalled replication forks. Nat Rev Mol Cell Biol (2006) 3.00
The DNA replication protein PriA and the recombination protein RecG bind D-loops. J Mol Biol (1997) 2.13
Accumulation of manganese in Neisseria gonorrhoeae correlates with resistance to oxidative killing by superoxide anion and is independent of superoxide dismutase activity. Mol Microbiol (2001) 1.73
Escherichia coli replication factor Y, a component of the primosome, can act as a DNA helicase. Proc Natl Acad Sci U S A (1987) 1.60
Continuous association of Escherichia coli single-stranded DNA binding protein with stable complexes of recA protein and single-stranded DNA. Biochemistry (1986) 1.54
Superoxide dismutase and oxygen toxicity defenses in the genus Neisseria. Infect Immun (1986) 1.54
PriA-directed assembly of a primosome on D loop DNA. J Biol Chem (1999) 1.47
Interactions of gonococci with phagocytic cells. Annu Rev Microbiol (1989) 1.43
The ordered assembly of the phiX174-type primosome. I. Isolation and identification of intermediate protein-DNA complexes. J Biol Chem (1996) 1.42
Effects of H2O2-producing lactobacilli on Neisseria gonorrhoeae growth and catalase activity. J Infect Dis (1994) 1.38
The ordered assembly of the phiX174-type primosome. III. PriB facilitates complex formation between PriA and DnaT. J Biol Chem (1996) 1.36
Association of phiX174 DNA-dependent ATPase activity with an Escherichia coli protein, replication factor Y, required for in vitro synthesis of phiX174 DNA. Proc Natl Acad Sci U S A (1975) 1.34
Two modes of PriA binding to DNA. J Biol Chem (1999) 1.28
Assembly of the primosome of DNA replication in Escherichia coli. J Biol Chem (1993) 1.28
Human neutrophil antimicrobial activity. Rev Infect Dis (1988) 1.28
A hand-off mechanism for primosome assembly in replication restart. Mol Cell (2007) 1.27
Neisseria gonorrhoeae DNA recombination and repair enzymes protect against oxidative damage caused by hydrogen peroxide. J Bacteriol (2006) 1.21
PriB stimulates PriA helicase via an interaction with single-stranded DNA. J Biol Chem (2005) 1.15
Mutation of the priA gene of Neisseria gonorrhoeae affects DNA transformation and DNA repair. J Bacteriol (2005) 1.12
Complexed crystal structure of replication restart primosome protein PriB reveals a novel single-stranded DNA-binding mode. Nucleic Acids Res (2006) 1.05
Crystal structure of PriB, a primosomal DNA replication protein of Escherichia coli. J Biol Chem (2004) 1.02
Crystal structure of a biologically functional form of PriB from Escherichia coli reveals a potential single-stranded DNA-binding site. Biochem Biophys Res Commun (2005) 1.02
Interactions of Escherichia coli replicative helicase PriA protein with single-stranded DNA. Biochemistry (2000) 1.02
Crystal structure of PriB, a component of the Escherichia coli replication restart primosome. Structure (2004) 0.98
Escherichia coli replicative helicase PriA protein-single-stranded DNA complex. Stoichiometries, free energy of binding, and cooperativities. J Biol Chem (2000) 0.98
Escherichia coli PriA helicase: fork binding orients the helicase to unwind the lagging strand side of arrested replication forks. J Mol Biol (2001) 0.97
Structural basis of the 3'-end recognition of a leading strand in stalled replication forks by PriA. EMBO J (2007) 0.96
Reverse transcriptase-PCR differential display analysis of meningococcal transcripts during infection of human cells: up-regulation of priA and its role in intracellular replication. BMC Microbiol (2008) 0.90
Interactions of the Escherichia coli primosomal PriB protein with the single-stranded DNA. Stoichiometries, intrinsic affinities, cooperativities, and base specificities. J Mol Biol (2010) 0.89
The crystal structure of Neisseria gonorrhoeae PriB reveals mechanistic differences among bacterial DNA replication restart pathways. Nucleic Acids Res (2009) 0.81
The crystal structure of Neisseria gonorrhoeae PriB reveals mechanistic differences among bacterial DNA replication restart pathways. Nucleic Acids Res (2009) 0.81
Conservation of the three-dimensional structure in non-homologous or unrelated proteins. Hum Genomics (2012) 0.78
Identification of a small molecule PriA helicase inhibitor. Biochemistry (2012) 0.76
The priB gene of Klebsiella pneumoniae encodes a 104-amino acid protein that is similar in structure and function to Escherichia coli PriB. PLoS One (2011) 0.75