The Bacillus subtilis primosomal protein DnaD untwists supercoiled DNA.
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Regulation of DNA Replication Initiation by Chromosome StructureStructure of the N-Terminal Oligomerization Domain of DnaD Reveals a Unique Tetramerization Motif and Provides Insights into Scaffold FormationPrimase is required for helicase activity and helicase alters the specificity of primase in the enteropathogen Clostridium difficileCharacterization of a novel non-specific nuclease from thermophilic bacteriophage GBSV1DnaC inactivation in Escherichia coli K-12 induces the SOS response and expression of nucleotide biosynthesis genesThe cyanobacterial cell division factor Ftn6 contains an N-terminal DnaD-like domainIntragenic and extragenic suppressors of temperature sensitive mutations in the replication initiation genes dnaD and dnaB of Bacillus subtilis.DnaB proteolysis in vivo regulates oligomerization and its localization at oriC in Bacillus subtilis.Biophysical characterization of DNA binding from single molecule force measurementsWhen simple sequence comparison fails: the cryptic case of the shared domains of the bacterial replication initiation proteins DnaB and DnaD.Characterization of Staphylococcus aureus Primosomal DnaD Protein: Highly Conserved C-Terminal Region Is Crucial for ssDNA and PriA Helicase Binding but Not for DnaA Protein-Binding and Self-TetramerizationReal-time detection of DNA topological changes with a fluorescently labeled cruciform.Loading mechanisms of ring helicases at replication origins.Chromosomal replication initiation machinery of low-G+C-content FirmicutesControl of Initiation of DNA Replication in Bacillus subtilis and Escherichia coli.Untwisting of the DNA helix stimulates the endonuclease activity of Bacillus subtilis Nth at AP sitesOrdered association of helicase loader proteins with the Bacillus subtilis origin of replication in vivo.Single-molecule atomic force spectroscopy reveals that DnaD forms scaffolds and enhances duplex melting.The primosomal protein DnaD inhibits cooperative DNA binding by the replication initiator DnaA in Bacillus subtilis.Primosomal proteins DnaD and DnaB are recruited to chromosomal regions bound by DnaA in Bacillus subtilisDeciphering the role of the AT-rich interaction domain and the HMG-box domain of ARID-HMG proteins of Arabidopsis thaliana.
P2860
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P2860
The Bacillus subtilis primosomal protein DnaD untwists supercoiled DNA.
description
2006 nî lūn-bûn
@nan
2006年の論文
@ja
2006年論文
@yue
2006年論文
@zh-hant
2006年論文
@zh-hk
2006年論文
@zh-mo
2006年論文
@zh-tw
2006年论文
@wuu
2006年论文
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2006年论文
@zh-cn
name
The Bacillus subtilis primosomal protein DnaD untwists supercoiled DNA.
@en
The Bacillus subtilis primosomal protein DnaD untwists supercoiled DNA.
@nl
type
label
The Bacillus subtilis primosomal protein DnaD untwists supercoiled DNA.
@en
The Bacillus subtilis primosomal protein DnaD untwists supercoiled DNA.
@nl
prefLabel
The Bacillus subtilis primosomal protein DnaD untwists supercoiled DNA.
@en
The Bacillus subtilis primosomal protein DnaD untwists supercoiled DNA.
@nl
P2860
P50
P356
P1476
The Bacillus subtilis primosomal protein DnaD untwists supercoiled DNA
@en
P2093
Wenke Zhang
P2860
P304
P356
10.1128/JB.00339-06
P407
P577
2006-08-01T00:00:00Z