| scholarly article | Q13442814 |
| P2093 | author name string | R Maurer | |
| L Stordal | |||
| P2860 | cites work | Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4 | Q25938983 |
| A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding | Q25938984 | ||
| Rapid and efficient site-specific mutagenesis without phenotypic selection | Q27860608 | ||
| Use of T7 RNA polymerase to direct expression of cloned genes | Q27860692 | ||
| Sequence from picomole quantities of proteins electroblotted onto polyvinylidene difluoride membranes | Q28131700 | ||
| Determination of molecular weights and frictional ratios of proteins in impure systems by use of gel filtration and density gradient centrifugation. Application to crude preparations of sulfite and hydroxylamine reductases | Q29618430 | ||
| Escherichia coli dnaB mutant defective in DNA initiation: isolation and properties of the dnaB protein | Q33961703 | ||
| A general priming system employing only dnaB protein and primase for DNA replication | Q33972532 | ||
| Primase, the dnaG protein of Escherichia coli. An enzyme which starts DNA chains | Q34049833 | ||
| Domains of Escherichia coli primase: functional activity of a 47-kDa N-terminal proteolytic fragment | Q35916786 | ||
| Purification and characterization of a mutant DnaB protein specifically defective in ATP hydrolysis | Q36136421 | ||
| Dominant lethal mutations in the dnaB helicase gene of Salmonella typhimurium | Q36211588 | ||
| A structural model for the Escherichia coli DnaB helicase based on electron microscopy data. | Q36693128 | ||
| Identification of a domain of Escherichia coli primase required for functional interaction with the DnaB helicase at the replication fork | Q38311133 | ||
| Primase from Escherichia coli primes single-stranded templates in the absence of single-stranded DNA-binding protein or other auxiliary proteins. Template sequence requirements based on the bacteriophage G4 complementary strand origin and Okazaki fr | Q38318265 | ||
| Enriched sources of Escherichia coli replication proteins. The dnaG primase is a zinc metalloprotein | Q38326619 | ||
| Biochemical characterization of Escherichia coli temperature-sensitive dnaB mutants dnaB8, dnaB252, dnaB70, dnaB43, and dnaB454 | Q39835760 | ||
| dnaB protein of Escherichia coli. Purification and role in the replication of phiX174 DNA | Q39838341 | ||
| The dnaB gene product of Escherichia coli. I. Purification, homogeneity, and physical properties | Q40146044 | ||
| The dnaB gene product of Escherichia coli. II. Single stranded DNA-dependent ribonucleoside triphosphatase activity | Q40146049 | ||
| Coordinated leading- and lagging-strand synthesis at the Escherichia coli DNA replication fork. I. Multiple effectors act to modulate Okazaki fragment size | Q43952441 | ||
| Cloning vectors that yield high levels of single-stranded DNA for rapid DNA sequencing | Q44209518 | ||
| Nucleotide sequence of dnaB and the primary structure of the dnaB protein from Escherichia coli | Q48393239 | ||
| Structure and function of Escherichia coli DnaB protein: role of the N-terminal domain in helicase activity. | Q54627242 | ||
| Defective replication activity of a dominant-lethal dnaB gene product from Escherichia coli. | Q54672778 | ||
| An over-expression plasmid for Escherichia coli primase. | Q54698323 | ||
| The HexamericE. coliDnaB Helicase can Exist in Different Quarternary States | Q56937904 | ||
| Helicase action of dnaB protein during replication from the Escherichia coli chromosomal origin in vitro | Q61959649 | ||
| The Escherichia coli dnaB replication protein is a DNA helicase | Q70134303 | ||
| Structural and functional studies of the dnaB protein using limited proteolysis. Characterization of domains for DNA-dependent ATP hydrolysis and for protein association in the primosome | Q70197469 | ||
| Oligomeric structure of Escherichia coli primary replicative helicase DnaB protein | Q72878683 | ||
| Mechanism of dnaB protein action. I. Crystallization and properties of dnaB protein, an essential replication protein in Escherichia coli | Q72891238 | ||
| Mechanism of dnaB protein action. II. ATP hydrolysis by dnaB protein dependent on single- or double-stranded DNA | Q72891242 | ||
| Mechanism of dnaB protein action. III. Allosteric role of ATP in the alteration of DNA structure by dnaB protein in priming replication | Q72891246 | ||
| Mechanism of dnaB protein action. IV. General priming of DNA replication by dnaB protein and primase compared with RNA polymerase | Q72891249 | ||
| P433 | issue | 15 | |
| P407 | language of work or name | English | Q1860 |
| P921 | main subject | Escherichia coli | Q25419 |
| P304 | page(s) | 4620-4627 | |
| P577 | publication date | 1996-08-01 | |
| P1433 | published in | Journal of Bacteriology | Q478419 |
| P1476 | title | Defect in general priming conferred by linker region mutants of Escherichia coli dnaB | |
| P478 | volume | 178 |
| Q27619052 | Crystal structure of the N-terminal domain of the DnaB hexameric helicase |
| Q36443377 | DnaC traps DnaB as an open ring and remodels the domain that binds primase. |
| Q47603277 | DnaC, the indispensable companion of DnaB helicase, controls the accessibility of DnaB helicase by primase |
| 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 |
| Q27650607 | Hexameric ring structure of the N-terminal domain of Mycobacterium tuberculosis DnaB helicase |
| Q43490099 | Identification of a region of Escherichia coli DnaB required for functional interaction with DnaG at the replication fork |
| Q43203582 | In the Bacillus stearothermophilus DnaB-DnaG complex, the activities of the two proteins are modulated by distinct but overlapping networks of residues |
| Q27619049 | NMR structure of the N-terminal domain of E. coli DnaB helicase: implications for structure rearrangements in the helicase hexamer |
| Q28357054 | Primase is required for helicase activity and helicase alters the specificity of primase in the enteropathogen Clostridium difficile |
| Q36153494 | The bacterial helicase-primase interaction: a common structural/functional module. |
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