Residues within the N-terminal Domain of Human Topoisomerase I Play a Direct Role in Relaxation*
Open Access
- 1 January 2001
- journal article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 276 (23), 20220-20227
- https://doi.org/10.1074/jbc.m010991200
Abstract
No abstract availableKeywords
This publication has 42 references indexed in Scilit:
- Catalytic Mechanism of DNA Topoisomerase IBMolecular Cell, 2000
- A Functional Linker in Human Topoisomerase I Is Required for Maximum Sensitivity to Camptothecin in a DNA Relaxation AssayPublished by Elsevier ,1999
- Crystal Structures of Human Topoisomerase I in Covalent and Noncovalent Complexes with DNAScience, 1998
- A Model for the Mechanism of Human Topoisomerase IScience, 1998
- Conservation of Structure and Mechanism between Eukaryotic Topoisomerase I and Site-Specific RecombinasesCell, 1998
- Alterations in the Catalytic Activity of Yeast DNA Topoisomerase I Result in Cell Cycle Arrest and Cell DeathPublished by Elsevier ,1997
- Biochemical and Biophysical Analyses of Recombinant Forms of Human Topoisomerase IPublished by Elsevier ,1996
- Purification and Characterization of Human Topoisomerase I MutantsEuropean Journal of Biochemistry, 1996
- The Domain Organization of Human Topoisomerase IJournal of Biological Chemistry, 1996
- Eukaryotic DNA topoisomerases: two forms of type I DNA topoisomerases from HeLa cell nuclei.Proceedings of the National Academy of Sciences, 1981