Interactions of the Escherichia coli primosomal PriB protein with the single-stranded DNA. Stoichiometries, intrinsic affinities, cooperativities, and base specificities.
about
Structural insight into the DNA-binding mode of the primosomal proteins PriA, PriB, and DnaTA bacterial PriB with weak single-stranded DNA binding activity can stimulate the DNA unwinding activity of its cognate PriA helicaseEnergetics of the Escherichia coli DnaT protein trimerization reaction.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.Full-length Dengue virus RNA-dependent RNA polymerase-RNA/DNA complexes: stoichiometries, intrinsic affinities, cooperativities, base, and conformational specificities.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-TetramerizationMacromolecular competition titration method accessing thermodynamics of the unmodified macromolecule-ligand interactions through spectroscopic titrations of fluorescent analogs.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 cofactorsThe Escherichia coli primosomal DnaT protein exists in solution as a monomer-trimer equilibrium systemQuantitative Thermodynamic Analyses of Spectroscopic Titration Curves.The primary DNA-binding subsite of the rat pol β. Energetics of interactions of the 8-kDa domain of the enzyme with the ssDNADnaT 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.
P2860
Q21284726-3B048AE3-8C9C-4B12-B53E-A37E9F4B06B8Q28485126-1791B3EF-9E71-451E-9F50-046D84946EEDQ30427360-44E6B2BA-089F-4C0C-9A5F-C836D19791F2Q34772969-60FE7F03-4F80-4C53-8570-CD62C58CE35EQ35311930-F6AA0C97-541E-4225-9DC7-41632BDE32BEQ36052744-FDAC5E45-5AAE-402D-89A2-14AA76A7D826Q38338367-F25795C9-8630-4711-9F8D-086BAAD90AA1Q38902746-A8EA2BFD-4EAF-4319-ADDD-1106571A5415Q41969856-16019388-75B2-4C87-A974-A24EE1BB0934Q42025314-7B09E918-F1A6-4475-9072-485EED5D3BC8Q42734673-E3FED9D3-BEC7-4704-AD1D-F264694FF6A1Q44902851-7ACE8D10-A86D-4CDD-A784-153D575FC3E7Q47334226-3BDE13BD-B0CF-4E59-9CA3-2432DCDFE6FCQ47734055-55153CCA-50E6-4533-A5C5-600E8727F2ED
P2860
Interactions of the Escherichia coli primosomal PriB protein with the single-stranded DNA. Stoichiometries, intrinsic affinities, cooperativities, and base specificities.
description
2010 nî lūn-bûn
@nan
2010年の論文
@ja
2010年論文
@yue
2010年論文
@zh-hant
2010年論文
@zh-hk
2010年論文
@zh-mo
2010年論文
@zh-tw
2010年论文
@wuu
2010年论文
@zh
2010年论文
@zh-cn
name
Interactions of the Escherichi ...... ities, and base specificities.
@en
Interactions of the Escherichi ...... ities, and base specificities.
@nl
type
label
Interactions of the Escherichi ...... ities, and base specificities.
@en
Interactions of the Escherichi ...... ities, and base specificities.
@nl
prefLabel
Interactions of the Escherichi ...... ities, and base specificities.
@en
Interactions of the Escherichi ...... ities, and base specificities.
@nl
P2860
P1476
Interactions of the Escherichi ...... vities, and base specificities
@en
P2093
Maria J Jezewska
Wlodzimierz Bujalowski
P2860
P356
10.1016/J.JMB.2010.02.009
P407
P577
2010-02-12T00:00:00Z