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Escherichia coli PriA helicase: fork binding orients the helicase to unwind the lagging strand side of arrested replication forks11Edited by M. Gottesman
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Rescue of stalled replication forks by RecG: Simultaneous translocation on the leading and lagging strand templates supports an active DNA unwinding model of fork reversal and Holliday junction formation
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The Disposition of Nascent Strands at Stalled Replication Forks Dictates the Pathway of Replisome Loading during Restart
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Escherichia coli factor Y sites of plasmid pBR322 can function as origins of DNA replication.
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Strand Displacement by DNA Polymerase III Occurs through a τ-ψ-χ Link to Single-stranded DNA-binding Protein Coating the Lagging Strand Template
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The Escherichia coli PriA Helicase–Double-Stranded DNA Complex: Location of the Strong DNA-Binding Subsite on the Helicase Domain of the Protein and the Affinity Control by the Two Nucleotide-Binding Sites of the Enzyme
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September 2010 |
Transcription leads to pervasive replisome instability in bacteria
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January 2017 |
The Escherichia Coli PriA Helicase Specifically Recognizes Gapped DNA Substrates
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February 2011 |
HLTF’s Ancient HIRAN Domain Binds 3′ DNA Ends to Drive Replication Fork Reversal
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June 2015 |
Structure of an OhrR-ohrA Operator Complex Reveals the DNA Binding Mechanism of the MarR Family
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October 2005 |
Interactions of Escherichia coli Replicative Helicase PriA Protein with Single-Stranded DNA †
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Integration, scaling, space-group assignment and post-refinement
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PriA mutations that affect PriA-PriC function during replication restart: PriA-PriC interactions
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August 2001 |
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Identification of Subunit Binding Positions on a Model Fork and Displacements That Occur during Sequential Assembly of the Escherichia coli Primosome
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March 2015 |
Modulation of recombination and DNA repair by the RecG and PriA helicases of Escherichia coli K-12.
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Structure of the SSB-DNA polymerase III interface and its role in DNA replication: SSB-replisome interaction
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An aromatic-rich loop couples DNA binding and ATP hydrolysis in the PriA DNA helicase
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August 2016 |
The PriA Replication Restart Protein Blocks Replicase Access Prior to Helicase Assembly and Directs Template Specificity through Its ATPase Activity
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December 2012 |
Measurement of SOS expression in individual Escherichia coli K-12 cells using fluorescence microscopy: SOS expression using fluorescence microscopy
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July 2004 |
Cavin1 intrinsically disordered domains are essential for fuzzy electrostatic interactions and caveola formation
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February 2021 |
PriA supports two distinct pathways for replication restart in UV-irradiated Escherichia coli cells: PriA-mediated rescue of stalled replication forks
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February 2003 |
A Critical Role of the 3′ Terminus of Nascent DNA Chains in Recognition of Stalled Replication Forks
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PriA-directed Assembly of a Primosome on D Loop DNA
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Properties of the PriA Helicase Domain and Its Role in Binding PriA to Specific DNA Structures
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Co-crystal structure of the HNF-3/fork head DNA-recognition motif resembles histone H5
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Crosslink Mapping at Amino Acid-Base Resolution Reveals the Path of Scrunched DNA in Initial Transcribing Complexes
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September 2015 |
The Escherichia coli PriA Helicase Specifically Recognizes Gapped DNA Substrates : EFFECT OF THE TWO NUCLEOTIDE-BINDING SITES OF THE ENZYME ON THE RECOGNITION PROCESS
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January 2010 |
Structural mechanisms of PriA-mediated DNA replication restart
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December 2013 |
PriA Mediates DNA Replication Pathway Choice at Recombination Intermediates
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PHENIX: a comprehensive Python-based system for macromolecular structure solution
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Mechanisms of bacterial DNA replication restart
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High-throughput, subpixel precision analysis of bacterial morphogenesis and intracellular spatio-temporal dynamics: Quantitative analysis of spatio-temporal dynamics
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Escherichia coli PriA Protein, Two Modes of DNA Binding and Activation of ATP Hydrolysis
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Specificity in suppression of SOS expression by recA4162 and uvrD303
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Genetic Location of Certain Mutations Conferring Recombination Deficiency in Escherichia coli
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Effects of mutations involving cell division, recombination, and chromosome dimer resolution on a priA2::kan mutant
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A Hand-Off Mechanism for Primosome Assembly in Replication Restart
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Benzophenone Triplet: a New Photochemical Probe of Biological Ligand-Receptor Interactions
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The importance of repairing stalled replication forks
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Structural basis of the 3′-end recognition of a leading strand in stalled replication forks by PriA
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Stabilization of a Stalled Replication Fork by Concerted Actions of Two Helicases
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December 2005 |
A novel dnaC mutation that suppresses priB rep mutant phenotypes in Escherichia coli K-12
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May 2006 |
Efficient incorporation of unnatural amino acids into proteins in Escherichia coli
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March 2006 |
Structural mechanisms of DNA binding and unwinding in bacterial RecQ helicases
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March 2015 |
Helicase-deficient cysteine to glycine substitution mutants of Escherichia coli replication protein PriA retain single-stranded DNA-dependent ATPase activity. Zn2+ stimulation of mutant PriA helicase and primosome assembly activities.
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February 1993 |
Multiple Genetic Pathways for Restarting DNA Replication Forks in Escherichia coli K-12
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June 2000 |