Structural basis of the 3'-end recognition of a leading strand in stalled replication forks by PriA. - Wikidata - awgldk - TriplyDB

Structural basis of the 3'-end recognition of a leading strand in stalled replication forks by PriA.

Structural basis of the 3'-end recognition of a leading strand in stalled replication forks by PriA.

http://www.wikidata.org/entity/Q35794344

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Structural insight into the DNA-binding mode of the primosomal proteins PriA, PriB, and DnaT Remodeling and Control of Homologous Recombination by DNA Helicases and Translocases that Target Recombinases and Synapsis Structural mechanisms of PriA-mediated DNA replication restart Crystal structure of DnaT 84–153 -dT10 ssDNA complex reveals a novel single-stranded DNA binding mode Structure 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 complex A bacterial PriB with weak single-stranded DNA binding activity can stimulate the DNA unwinding activity of its cognate PriA helicase The Escherichia coli PriA helicase specifically recognizes gapped DNA substrates: effect of the two nucleotide-binding sites of the enzyme on the recognition process.Identification of Subunit Binding Positions on a Model Fork and Displacements That Occur during Sequential Assembly of the Escherichia coli Primosome.HLTF's Ancient HIRAN Domain Binds 3' DNA Ends to Drive Replication Fork Reversal.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-Tetramerization PriC-mediated DNA replication restart requires PriC complex formation with the single-stranded DNA-binding protein.Characterization of the ATPase activity of RecG and RuvAB proteins on model fork structures reveals insight into stalled DNA replication fork repair An aromatic-rich loop couples DNA binding and ATP hydrolysis in the PriA DNA helicase.Recruitment to stalled replication forks of the PriA DNA helicase and replisome-loading activities is essential for survival.The N-terminal domain of the Escherichia coli PriA helicase contains both the DNA- and nucleotide-binding sites. Energetics of domain--DNA interactions and allosteric effect of the nucleotide cofactors Replication Restart in Bacteria.Different genome stability proteins underpin primed and naïve adaptation in E. coli CRISPR-Cas immunity.A priA Mutant Expressed in Two Pieces Has Almost Full Activity in Escherichia coli K-12.The replication-transcription conflict Domain separation and characterization of PriC, a replication restart primosome factor in Escherichia coli.DnaT is a single-stranded DNA binding protein.Mechanisms of bacterial DNA replication restart.Yeast two-hybrid analysis of PriB-interacting proteins in replication restart primosome: a proposed PriB-SSB interaction model.Basic and aromatic residues in the C-terminal domain of PriC are involved in ssDNA and SSB binding.Structure-specific DNA replication-fork recognition directs helicase and replication restart activities of the PriA helicase

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P2860

Structural basis of the 3'-end recognition of a leading strand in stalled replication forks by PriA.

http://www.wikidata.org/entity/Q35794344

description

2007 nî lūn-bûn

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2007年の論文

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2007年論文

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2007年論文

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2007年論文

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2007年論文

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2007年論文

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2007年论文

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2007年论文

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Structural basis of the 3'-end ...... led replication forks by PriA.

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Structural basis of the 3'-end ...... led replication forks by PriA.

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Structural basis of the 3'-end ...... led replication forks by PriA.

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Structural basis of the 3'-end ...... led replication forks by PriA.

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Structural basis of the 3'-end ...... led replication forks by PriA.

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Structural basis of the 3'-end ...... led replication forks by PriA.

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SJ.EMBOJ.7601697

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The EMBO Journal

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Structural basis of the 3'-end ...... led replication forks by PriA.

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P2093

Daisuke Kohda

http://www.w3.org/2001/XMLSchema#string

Hisao Masai

http://www.w3.org/2001/XMLSchema#string

Kaori Sasaki

http://www.w3.org/2001/XMLSchema#string

Katsumi Maenaka

http://www.w3.org/2001/XMLSchema#string

Mihoko Saito

http://www.w3.org/2001/XMLSchema#string

Naoaki Okamoto

http://www.w3.org/2001/XMLSchema#string

Taku Tanaka

http://www.w3.org/2001/XMLSchema#string

Toyoyuki Ose

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Tsuyoshi Shirai

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P2860

Improved methods for building protein models in electron density maps and the location of errors in these models

Crystallography & NMR System: A New Software Suite for Macromolecular Structure Determination

Structural basis for FEN-1 substrate specificity and PCNA-mediated activation in DNA replication and repair

Automated protein model building combined with iterative structure refinement

Touring protein fold space with Dali/FSSP

Automated MAD and MIR structure solution

Initiation of genetic recombination and recombination-dependent replication

Structural basis of 3' end RNA recognition and exoribonucleolytic cleavage by an exosome RNase PH core

Automated structure solution, density modification and model building

Amino acid-base interactions: a three-dimensional analysis of protein-DNA interactions at an atomic level

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2584-2593

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10

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26

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2007-04-26T00:00:00Z

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6365599

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17464287

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1868909

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