Assembly of the bacteriophage T4 helicase: architecture and stoichiometry of the gp41-gp59 complex.
about
Unraveling DNA helicases. Motif, structure, mechanism and functionCoordinated DNA Replication by the Bacteriophage T4 ReplisomeStructural analysis of Bacillus subtilis SPP1 phage helicase loader protein G39PCoupling DNA unwinding activity with primer synthesis in the bacteriophage T4 primosomeInvestigation of stoichiometry of T4 bacteriophage helicase loader protein (gp59)Structural features of covalently cross-linked hydroxylase and reductase proteins of soluble methane monooxygenase as revealed by mass spectrometric analysis.Assembly of the bacteriophage T4 primosome: single-molecule and ensemble studiesBacteriophage T4 helicase loader protein gp59 functions as gatekeeper in origin-dependent replication in vivo.Isothermal DNA amplification using the T4 replisome: circular nicking endonuclease-dependent amplification and primase-based whole-genome amplification'Modulation of the enzymatic activities of replicative helicase (DnaB) by interaction with Hp0897: a possible mechanism for helicase loading in Helicobacter pylori'.DNA unwinding by ring-shaped T4 helicase gp41 is hindered by tension on the occluded strandArp2/3 complex is bound and activated by two WASP proteins.Mutational analysis of the T4 gp59 helicase loader reveals its sites for interaction with helicase, single-stranded binding protein, and DNAModels for the binary complex of bacteriophage T4 gp59 helicase loading protein: gp32 single-stranded DNA-BINDING protein and ternary complex with pseudo-Y junction DNA.Assembly and dynamics of Gp59-Gp32-single-stranded DNA (ssDNA), a DNA helicase loading complex required for recombination-dependent replication in bacteriophage T4Nonradioactive, ultrasensitive site-specific protein-protein photocrosslinking: interactions of alpha-helix 2 of TATA-binding protein with general transcription factor TFIIA and transcriptional repressor NC2.Control of helicase loading in the coupled DNA replication and recombination systems of bacteriophage T4.Assembly and dynamics of the bacteriophage T4 homologous recombination machinery.A CDC6-like factor from the archaea Sulfolobus solfataricus promotes binding of the mini-chromosome maintenance complex to DNA.Protein-protein interactions in the bacteriophage T4 replisome. The leading strand holoenzyme is physically linked to the lagging strand holoenzyme and the primosome.Understanding DNA replication by the bacteriophage T4 replisome.Dual functions of single-stranded DNA-binding protein in helicase loading at the bacteriophage T4 DNA replication fork.Mutations of bacteriophage T4 59 helicase loader defective in binding fork DNA and in interactions with T4 32 single-stranded DNA-binding protein.Site-directed mutations of T4 helicase loading protein (gp59) reveal multiple modes of DNA polymerase inhibition and the mechanism of unlocking by gp41 helicase.Dissociative properties of the proteins within the bacteriophage T4 replisome.The application of a minicircle substrate in the study of the coordinated T4 DNA replication.
P2860
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P2860
Assembly of the bacteriophage T4 helicase: architecture and stoichiometry of the gp41-gp59 complex.
description
2002 nî lūn-bûn
@nan
2002 թուականի Ապրիլին հրատարակուած գիտական յօդուած
@hyw
2002 թվականի ապրիլին հրատարակված գիտական հոդված
@hy
2002年の論文
@ja
2002年論文
@yue
2002年論文
@zh-hant
2002年論文
@zh-hk
2002年論文
@zh-mo
2002年論文
@zh-tw
2002年论文
@wuu
name
Assembly of the bacteriophage ...... etry of the gp41-gp59 complex.
@ast
Assembly of the bacteriophage ...... etry of the gp41-gp59 complex.
@en
type
label
Assembly of the bacteriophage ...... etry of the gp41-gp59 complex.
@ast
Assembly of the bacteriophage ...... etry of the gp41-gp59 complex.
@en
prefLabel
Assembly of the bacteriophage ...... etry of the gp41-gp59 complex.
@ast
Assembly of the bacteriophage ...... etry of the gp41-gp59 complex.
@en
P2093
P2860
P356
P1476
Assembly of the bacteriophage ...... etry of the gp41-gp59 complex.
@en
P2093
Faoud T Ishmael
Stephen C Alley
Stephen J Benkovic
P2860
P304
20555-20562
P356
10.1074/JBC.M111951200
P407
P577
2002-04-01T00:00:00Z