Role of DNA intercalators in the binding of RecA to double-stranded DNA
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry
Reference33 articles.
1. Kinetic studies of recA protein binding to a fluorescent single-stranded polynucleotide
2. Cofactor-induced orientation of the DNA bases in single-stranded DNA complexed with RecA protein. A fluorescence anisotropy and time-decay study.
3. The structure of recA protein-DNA filaments. 2 recA protein monomers unwind 17 base pairs of DNA by 11.5 degrees/base pair in the presence of adenosine 5'-O-(3-thiotriphosphate).
4. The location of DNA in complexes of recA protein with double-stranded DNA. A neutron scattering study
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1. Direct visualization of the formation of RecA/dsDNA complexes at the single-molecule level;Micron;2012-10
2. Influence of Polyelectrolyte on DNA-RecA Nucleoprotein Filaments: Poly-L-Lysine Used as a Model;ChemPhysChem;2009-07-13
3. Gene targeting in mouse embryos mediated by RecA and modified single-stranded oligonucleotides;In Vitro Cellular & Developmental Biology - Animal;2008-02-12
4. Structural analysis of RecA protein–DNA complexes by fluorescence-detected linear dichroism: Absence of structural change of filament for pairing of complementary DNA strands;Analytical Biochemistry;2006-11
5. Investigating Structural Changes Induced By Nucleotide Binding to RecA Using Difference FTIR;Biophysical Journal;2002-04
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