| scholarly article | Q13442814 |
| P50 | author | Panos Soultanas | Q38317689 |
| P2093 | author name string | Christopher Anderson | |
| Laurence Gardiner | |||
| Stephanie Allen | |||
| Anna Haroniti | |||
| Clive J Roberts | |||
| Zara Doddridge | |||
| P2860 | cites work | NMR structure of the N-terminal domain of E. coli DnaB helicase: implications for structure rearrangements in the helicase hexamer | Q27619049 |
| Crystal structure of the N-terminal domain of the DnaB hexameric helicase | Q27619052 | ||
| Mechanism of processivity clamp opening by the delta subunit wrench of the clamp loader complex of E. coli DNA polymerase III | Q27634545 | ||
| Crystal structure of the processivity clamp loader gamma (gamma) complex of E. coli DNA polymerase III | Q27634553 | ||
| Atomic structure of the clamp loader small subunit from Pyrococcus furiosus | Q27634751 | ||
| Flexibility of the rings: structural asymmetry in the DnaB hexameric helicase | Q30309878 | ||
| From images to interactions: high-resolution phase imaging in tapping-mode atomic force microscopy | Q30503591 | ||
| Two essential DNA polymerases at the bacterial replication fork. | Q33183142 | ||
| The gamma subunit of DNA polymerase III holoenzyme of Escherichia coli is produced by ribosomal frameshifting | Q33580719 | ||
| Devoted to the lagging strand-the subunit of DNA polymerase III holoenzyme contacts SSB to promote processive elongation and sliding clamp assembly | Q33888734 | ||
| Opening of the clamp: an intimate view of an ATP-driven biological machine. | Q34381828 | ||
| Programmed translational frameshifting. | Q34412357 | ||
| Clamp-loader-helicase interaction in Bacillus. Leucine 381 is critical for pentamerization and helicase binding of the Bacillus tau protein | Q34555120 | ||
| A novel assembly mechanism for the DNA polymerase III holoenzyme DnaX complex: association of deltadelta' with DnaX(4) forms DnaX(3)deltadelta'. | Q34681537 | ||
| Programmed ribosomal frameshifting generates the Escherichia coli DNA polymerase III gamma subunit from within the tau subunit reading frame | Q35834867 | ||
| ATP-dependent structural change of the eukaryotic clamp-loader protein, replication factor C. | Q35835905 | ||
| Direct physical interaction between DnaG primase and DnaB helicase of Escherichia coli is necessary for optimal synthesis of primer RNA. | Q36685433 | ||
| Nonlinearity in genetic decoding: homologous DNA replicase genes use alternatives of transcriptional slippage or translational frameshifting | Q37113313 | ||
| tau binds and organizes Escherichia coli replication proteins through distinct domains. Domain IV, located within the unique C terminus of tau, binds the replication fork, helicase, DnaB. | Q38306684 | ||
| tau binds and organizes Escherichia coli replication through distinct domains. Partial proteolysis of terminally tagged tau to determine candidate domains and to assign domain V as the alpha binding domain | Q38306688 | ||
| The chi psi subunits of DNA polymerase III holoenzyme bind to single-stranded DNA-binding protein (SSB) and facilitate replication of an SSB-coated template | Q38333951 | ||
| Coupling of a replicative polymerase and helicase: a tau-DnaB interaction mediates rapid replication fork movement | Q38361453 | ||
| Mapping protein-protein interactions within a stable complex of DNA primase and DnaB helicase from Bacillus stearothermophilus. | Q38642649 | ||
| Site-directed mutagenesis reveals roles for conserved amino acid residues in the hexameric DNA helicase DnaB from Bacillus stearothermophilus | Q39687119 | ||
| Bacillus subtilis tau subunit of DNA polymerase III interacts with bacteriophage SPP1 replicative DNA helicase G40P. | Q39689763 | ||
| Translational frame shifting in theEscherichia colidnaX genein vitro | Q40510217 | ||
| The DNA replication machine of a gram-positive organism. | Q47235544 | ||
| The HexamericE. coliDnaB Helicase can Exist in Different Quarternary States | Q56937904 | ||
| The discrimination of IgM and IgG type antibodies and Fab′ and F(ab)2 antibody fragments on an industrial substrate using scanning force microscopy | Q58622706 | ||
| High-efficiency transformation of yeast by electroporation | Q70120808 | ||
| Mechanism of the E. coli tau processivity switch during lagging-strand synthesis | Q73086540 | ||
| Interaction between yeast RNA polymerase III and transcription factor TFIIIC via ABC10alpha and tau131 subunits | Q73176075 | ||
| The DnaX-binding subunits delta' and psi are bound to gamma and not tau in the DNA polymerase III holoenzyme | Q73396441 | ||
| Thermus thermophilis dnaX homolog encoding gamma- and tau-like proteins of the chromosomal replicase | Q73813717 | ||
| tau binds and organizes Escherichia coli replication proteins through distinct domains: domain III, shared by gamma and tau, oligomerizes DnaX | Q74236552 | ||
| Three-dimensional reconstructions from cryoelectron microscopy images reveal an intimate complex between helicase DnaB and its loading partner DnaC | Q74486176 | ||
| A three-domain structure for the delta subunit of the DNA polymerase III holoenzyme delta domain III binds delta' and assembles into the DnaX complex | Q77542579 | ||
| Trading places on DNA--a three-point switch underlies primer handoff from primase to the replicative DNA polymerase | Q78170535 | ||
| P433 | issue | 2 | |
| P407 | language of work or name | English | Q1860 |
| P304 | page(s) | 381-393 | |
| P577 | publication date | 2004-02-01 | |
| P1433 | published in | Journal of Molecular Biology | Q925779 |
| P1476 | title | The clamp-loader-helicase interaction in Bacillus. Atomic force microscopy reveals the structural organisation of the DnaB-tau complex in Bacillus | |
| P478 | volume | 336 |
| Q33439070 | Allosteric regulation of the primase (DnaG) activity by the clamp-loader (tau) in vitro. |
| Q57753310 | Bacillus subtilis RarA modulates replication restart |
| Q34953383 | Breaking the rules: bacteria that use several DNA polymerase IIIs |
| Q34555120 | Clamp-loader-helicase interaction in Bacillus. Leucine 381 is critical for pentamerization and helicase binding of the Bacillus tau protein |
| Q40969310 | DnaG interacts with a linker region that joins the N- and C-domains of DnaB and induces the formation of 3-fold symmetric rings |
| Q34558338 | Domain swapping reveals that the C- and N-terminal domains of DnaG and DnaB, respectively, are functional homologues |
| Q27677022 | Insights into the structure and assembly of the Bacillus subtilis clamp-loader complex and its interaction with the replicative helicase |
| Q27681112 | Nucleotide and Partner-Protein Control of Bacterial Replicative Helicase Structure and Function |
| Q28357054 | Primase is required for helicase activity and helicase alters the specificity of primase in the enteropathogen Clostridium difficile |
| Q27644566 | Solution structure of Domains IVa and V of the subunit of Escherichia coli DNA polymerase III and interaction with the subunit |
| Q38327850 | Solution structure of the helicase-interaction domain of the primase DnaG: a model for helicase activation. |
| Q27676744 | Structure of the PolIIIα-τc-DNA Complex Suggests an Atomic Model of the Replisome |
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