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Structural basis of replication origin recognition by the DnaA proteinThe interaction of DiaA and DnaA regulates the replication cycle in E. coli by directly promoting ATP DnaA-specific initiation complexesA common mechanism for the ATP-DnaA-dependent formation of open complexes at the replication originStructure and mechanism of the primosome protein DnaT-functional structures for homotrimerization, dissociation of ssDNA from the PriB·ssDNA complex, and formation of the DnaT·ssDNA complexDnaA binding locus datA promotes DnaA-ATP hydrolysis to enable cell cycle-coordinated replication initiation.Cooperative DnaA Binding to the Negatively Supercoiled datA Locus Stimulates DnaA-ATP Hydrolysis.Differentiation of the DnaA-oriC subcomplex for DNA unwinding in a replication initiation complex.Feedback controls restrain the initiation of Escherichia coli chromosomal replication.DiaA, a novel DnaA-binding protein, ensures the timely initiation of Escherichia coli chromosome replication.Timely binding of IHF and Fis to DARS2 regulates ATP-DnaA production and replication initiation.Specific binding of eukaryotic ORC to DNA replication origins depends on highly conserved basic residues.Functional analysis of CedA based on its structure: residues important in binding of DNA and RNA polymerase and in the cell division regulation.Near-atomic structural model for bacterial DNA replication initiation complex and its functional insights.DnaA, ORC, and Cdc6: similarity beyond the domains of life and diversity.Site-Specific Turn-On Fluorescent Labeling of DNA-Interacting Protein Using Oligodeoxynucleotides That Modify Lysines To Produce 5,6-Dimethoxy 3-Methyleneisoindolin-1-one.Bioconjugation of Oligodeoxynucleotides Carrying 1,4-Dicarbonyl Groups via Reductive Amination with Lysine Residues.Involvement of histidine in complex formation of PriB and single-stranded DNA.Crystal structure of a biologically functional form of PriB from Escherichia coli reveals a potential single-stranded DNA-binding site.Site-directed mutational analysis for the ATP binding of DnaA protein. Functions of two conserved amino acids (Lys-178 and Asp-235) located in the ATP-binding domain of DnaA protein in vitro and in vivo.Molecular mechanism of DNA replication-coupled inactivation of the initiator protein in Escherichia coli: interaction of DnaA with the sliding clamp-loaded DNA and the sliding clamp-Hda complex.Identification of the region in Escherichia coli DnaA protein required for specific recognition of the DnaA box.DnaA protein DNA-binding domain binds to Hda protein to promote inter-AAA+ domain interaction involved in regulatory inactivation of DnaA.The Escherichia coli Cryptic Prophage Protein YfdR Binds to DnaA and Initiation of Chromosomal Replication Is Inhibited by Overexpression of the Gene Cluster yfdQ-yfdR-yfdS-yfdTThe nucleoid protein H-NS facilitates chromosome DNA replication in Escherichia coli dnaA mutants.Long inverted repeat transiently stalls DNA replication by forming hairpin structures on both leading and lagging strands.Rapid Purification and Characterization of Mutant Origin Recognition Complexes in Saccharomyces cerevisiae.The Arg Fingers of Key DnaA Protomers Are Oriented Inward within the Replication Origin oriC and Stimulate DnaA Subcomplexes in the Initiation ComplexDiaA dynamics are coupled with changes in initial origin complexes leading to helicase loading.The DnaA homolog of the hyperthermophilic eubacterium Thermotoga maritima forms an open complex with a minimal 149-bp origin region in an ATP-dependent manner.DNA polymerase IV mediates efficient and quick recovery of replication forks stalled at N2-dG adductsHda monomerization by ADP binding promotes replicase clamp-mediated DnaA-ATP hydrolysis.Determination of the secondary structure in solution of the Escherichia coli DnaA DNA-binding domain.Domain separation and characterization of PriC, a replication restart primosome factor in Escherichia coli.Reactivation of DnaA by DNA sequence-specific nucleotide exchange in vitro.Regulatory dynamics in the ternary DnaA complex for initiation of chromosomal replication in Escherichia coli.Formation of an ATP-DnaA-specific initiation complex requires DnaA Arginine 285, a conserved motif in the AAA+ protein family.DnaA protein is sensitive to a soluble factor and is specifically inactivated for initiation of in vitro replication of the Escherichia coli minichromosome.Roles for the AAA+ motifs of DnaA in the initiation of DNA replication.Involvement of the Escherichia coli folate-binding protein YgfZ in RNA modification and regulation of chromosomal replication initiation.The DnaA N-terminal domain interacts with Hda to facilitate replicase clamp-mediated inactivation of DnaA.
P50
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P50
description
researcher
@en
wetenschapper
@nl
հետազոտող
@hy
name
Tsutomu Katayama
@ast
Tsutomu Katayama
@en
Tsutomu Katayama
@es
Tsutomu Katayama
@nl
type
label
Tsutomu Katayama
@ast
Tsutomu Katayama
@en
Tsutomu Katayama
@es
Tsutomu Katayama
@nl
prefLabel
Tsutomu Katayama
@ast
Tsutomu Katayama
@en
Tsutomu Katayama
@es
Tsutomu Katayama
@nl
P106
P1153
7401478446
P31
P496
0000-0001-9994-1684