Helicase-appended Topoisomerases: New Insight into the Mechanism of Directional Strand Transfer
Open Access
- 1 November 2009
- journal article
- review article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 284 (45) , 30737-30741
- https://doi.org/10.1074/jbc.r109.051268
Abstract
No abstract availableKeywords
This publication has 35 references indexed in Scilit:
- Adaptations to Submarine Hydrothermal Environments Exemplified by the Genome of Nautilia profundicolaPLoS Genetics, 2009
- The reverse gyrase helicase-like domain is a nucleotide-dependent switch that is attenuated by the topoisomerase domainNucleic Acids Research, 2008
- Functional Role of BLAP75 in BLM-Topoisomerase IIIα-dependent Holliday Junction ProcessingJournal of Biological Chemistry, 2008
- Resolution of Converging Replication Forks by RecQ and Topoisomerase IIIMolecular Cell, 2008
- Topoisomerase IIIα and Bloom’s helicase can resolve a mobile double Holliday junction substrate through convergent branch migrationProceedings of the National Academy of Sciences, 2006
- Reverse Gyrase Functions as a DNA RenaturaseJournal of Biological Chemistry, 2006
- Roles of the Bloom's syndrome helicase in the maintenance of genome stabilityBiochemical Society Transactions, 2005
- Drosophila melanogaster Topoisomerase IIIα Preferentially Relaxes a Positively or Negatively Supercoiled Bubble Substrate and Is Essential during DevelopmentJournal of Biological Chemistry, 2005
- RecQ Helicase and Topoisomerase III Comprise a Novel DNA Strand Passage FunctionMolecular Cell, 1999
- Bacterial DNA topoisomerase I can relax positively supercoiled DNA containing a single-stranded loopJournal of Molecular Biology, 1985