DnaC protein contains a modified ATP-binding motif and belongs to a novel family of ATPases including also DnaA.
about
The DNA binding domain of the initiator protein DnaAA common set of conserved motifs in a vast variety of putative nucleic acid-dependent ATPases including MCM proteins involved in the initiation of eukaryotic DNA replicationMechanisms for initiating cellular DNA replicationStructural Synergy and Molecular Crosstalk between Bacterial Helicase Loaders and Replication InitiatorsThe interaction of bacteriophage P2 B protein with Escherichia coli DnaB helicase.DnaD protein of Bacillus subtilis interacts with DnaA, the initiator protein of replicationGain-of-function mutations in TnsC, an ATP-dependent transposition protein that activates the bacterial transposon Tn7Early steps of Bacillus subtilis primosome assembly.Replication initiation at the Escherichia coli chromosomal originFunctional dissection of YabA, a negative regulator of DNA replication initiation in Bacillus subtilis'Modulation of the enzymatic activities of replicative helicase (DnaB) by interaction with Hp0897: a possible mechanism for helicase loading in Helicobacter pylori'.DNA-mediated transformation of bloodstream-form Trypanosoma brucei.Motors and switches: AAA+ machines within the replisome.Helicase binding to DnaI exposes a cryptic DNA-binding site during helicase loading in Bacillus subtilis.Genetic method to analyze essential genes of Escherichia coliSubstitutions of Conserved Residues in the C-terminal Region of DnaC Cause Thermolability in Helicase Loading.The bacterial DnaC helicase loader is a DnaB ring breaker.Loading mechanisms of ring helicases at replication origins.Mechanisms for initiating cellular DNA replication.A functional interaction between the putative primosomal protein DnaI and the main replicative DNA helicase DnaB in Bacillus.Restart of DNA replication in Gram-positive bacteria: functional characterisation of the Bacillus subtilis PriA initiator.The DnaC helicase loader is a dual ATP/ADP switch protein.Transposition of the IS21-related element IS1415 in Rhodococcus erythropolis.An Atypical AAA+ ATPase Assembly Controls Efficient Transposition through DNA Remodeling and Transposase Recruitment.Quantitative analysis of nucleotide modulation of DNA binding by DnaC protein of Escherichia coli.The interaction domains of the DnaA and DnaB replication proteins of Escherichia coli.
P2860
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P2860
DnaC protein contains a modified ATP-binding motif and belongs to a novel family of ATPases including also DnaA.
description
1992 nî lūn-bûn
@nan
1992 թուականի Ապրիլին հրատարակուած գիտական յօդուած
@hyw
1992 թվականի ապրիլին հրատարակված գիտական հոդված
@hy
1992年の論文
@ja
1992年論文
@yue
1992年論文
@zh-hant
1992年論文
@zh-hk
1992年論文
@zh-mo
1992年論文
@zh-tw
1992年论文
@wuu
name
DnaC protein contains a modifi ...... f ATPases including also DnaA.
@ast
DnaC protein contains a modifi ...... f ATPases including also DnaA.
@en
type
label
DnaC protein contains a modifi ...... f ATPases including also DnaA.
@ast
DnaC protein contains a modifi ...... f ATPases including also DnaA.
@en
prefLabel
DnaC protein contains a modifi ...... f ATPases including also DnaA.
@ast
DnaC protein contains a modifi ...... f ATPases including also DnaA.
@en
P2860
P356
P1476
DnaC protein contains a modifi ...... f ATPases including also DnaA.
@en
P2860
P356
10.1093/NAR/20.8.1997
P407
P577
1992-04-01T00:00:00Z