Kinetic Measurement of the Step Size of DNA Unwinding by Bacteriophage T7 DNA Helicase gp4
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Kim, Dong-Eun (Department of Biotechnology and Bioengineering, Dong-Eui University) |
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Rep protein as a helicase in an active, isolatable repolication fork of duplex phi X174 DNA
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Large scale purification and biochemical characterization of T7 primase/helicase proteins. Evidence for homodimer and heterodimer formation
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3 |
Kinetics and processivity of ATP hydrolysis and DNA unwinding by the RecBC enzyme from Escherichia coli
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DOI ScienceOn |
4 |
Characterization of the helicase activity of the Escherichia coli RecBCD enzyme using a novel helicase assay
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DOI ScienceOn |
5 |
Bacteriophage T7 DNA helicase binds dTTP forms hexamers, and binds DNA in the absence of Mg<TEX>$^{2+}$</TEX>. The presence of dTTP is sufficient for hexamer formation and DNA binding
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DOI ScienceOn |
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Kinetics of the RNA-DNA helicase activity of Escherichia coli transcription termination factor rho. 2. Processivity, ATP consumption, and RNA binding
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DOI ScienceOn |
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DNA is bound within the central hole to one or two of the six subunits of the T7 DNA helicase
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DOI ScienceOn |
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An oligomeric form of E. coli UvrD is required for optimal helicase activity
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DOI ScienceOn |
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The Escherichia coli dnaB replication protein in a DNA helicase
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10 |
Characterization of the adenosinetriphosphatase activity of the Escherichia coli RecBCD enzyme: relationship of ATP hydrolysis to the unwinding of duplex DNA
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DOI ScienceOn |
11 |
Processivity of the DNA helicase activity of Escherichia coli recBCD enzyme
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12 |
Domonstration of unidirectional single-stranded DNA translocation by PcrA helicase: measurement of step size and translocation speed
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DOI ScienceOn |
13 |
The DExH protein NPH-Ⅱ is a processive and directional motor for unwinding RNA
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DOI ScienceOn |
14 |
Kinetic measurement of the step size of DNA unwinding by Escherichia coil UvrD helicase
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DOI ScienceOn |
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Mechanisms of helicase-catalyzed DNA unwinding
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DOI ScienceOn |
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Single-turnover kinetics of helicase-catalyzed DNA unwinding monitored continuously by fluoresence energy transfer
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DOI ScienceOn |
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18 |
A ring-opening mechanism for DNA binding in the central channel of the T7 helicase-primase protein
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DOI ScienceOn |
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Helicase action of dnaB protein during replication from the Escherichia coli chromosomal origin in vitro
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Structure and Function of Hexameric Helicases
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DOI ScienceOn |
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Bacteriophage T7 helicase/primase proteins form rings around single-stranded DNA that suggest a general structure for hexameric helicases
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DOI ScienceOn |
22 |
T7 DNA helicase: a molecular motor that processively and unidirectionally translocates along single-stranded DNA
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DOI ScienceOn |
23 |
Asymmetric interactions of hexameric bacteriophage T7 DNA helicase with the 5'-and 3'-tails of the forked DNA substrate
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DOI ScienceOn |
24 |
Single stranded, Filamentous Bacteriophage Vectors
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A hexameric helicase encircles one DNA strand and excludes the other during DNA unwinding
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DOI ScienceOn |
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Cooperative interactions of nucleotide ligands are linked to oligomerization and DNA binding in bacteriophage T7 gene 4 helicases
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DOI ScienceOn |
27 |
Efficiency of ATP hydrolysis and DNA unwinding by the RecBC enzyme from Escherichia coli
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DOI ScienceOn |
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