Global Conformational Transitions in Escherichia coli Primary Replicative Helicase DnaB Protein Induced by ATP, ADP, and Single-stranded DNA Binding
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry
Reference23 articles.
1. Mechanism of dnaB protein action. II. ATP hydrolysis by dnaB protein dependent on single- or double-stranded DNA.
2. Mechanism of dnaB protein action. III. Allosteric role of ATP in the alteration of DNA structure by dnaB protein in priming replication.
3. Helicase action of dnaB protein during replication from the Escherichia coli chromosomal origin in vitro.
4. Negative cooperativity in the binding of nucleotides to Escherichia coli replicative helicase DnaB protein. Interactions with fluorescent nucleotide analogs
5. Structural Characteristics of the Nucleotide-Binding Site of Escherichia coli Primary Replicative Helicase DnaB Protein. Studies with Ribose and Base-Modified Fluorescent Nucleotide Analogs
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1. Replication | DNA Helicases: Hexameric Enzyme Action;Encyclopedia of Biological Chemistry III;2021
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3. Lambda gpP-DnaB Helicase Sequestration and gpP-RpoB Associated Effects: On Screens for Auxotrophs, Selection for RifR, Toxicity, Mutagenicity, Plasmid Curing;Viruses;2016-06-22
4. A Nucleotide-dependent and HRDC Domain-dependent Structural Transition in DNA-bound RecQ Helicase;Journal of Biological Chemistry;2014-02
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