Proteolytic Footprinting of Vaccinia Topoisomerase Bound to DNA
Open Access
- 1 May 1995
- journal article
- research article
- Published by Elsevier
- Vol. 270 (19) , 11636-11645
- https://doi.org/10.1074/jbc.270.19.11636
Abstract
No abstract availableKeywords
This publication has 11 references indexed in Scilit:
- Protein footprinting by the combined use of reversible and irreversible lysine modifications.Proceedings of the National Academy of Sciences, 1994
- Crystal structure of the amino-terminal fragment of vaccinia virus DNA topoisomerase I at 1.6 å resolutionStructure, 1994
- Requirements for noncovalent binding of vaccinia topoisomerase I to duplex DNANucleic Acids Research, 1994
- Study of allosteric communication between protomers by immunotaggingNature, 1993
- Proteolysis patterns of epitopically labeled yeast DNA topoisomerase II suggest an allosteric transition in the enzyme induced by ATP binding.Proceedings of the National Academy of Sciences, 1991
- The C-terminal domain of theEscherichia coliDNA gyrase A subunit is a DNA-binding proteinNucleic Acids Research, 1991
- Mapping the active-site tyrosine of vaccinia virus DNA topoisomerase I.Proceedings of the National Academy of Sciences, 1989
- Examination of automated polypeptide sequencing using standard phenyl isothiocyanate reagent and subpicomole high-performance liquid chromatographic analysisAnalytical Biochemistry, 1989
- Peptide sequencing and site-directed mutagenesis identify tyrosine-727 as the active site tyrosine of Saccharomyces cerevisiae DNA topoisomerase I.Proceedings of the National Academy of Sciences, 1989
- Identification of a vaccinia virus gene encoding a type I DNA topoisomerase.Proceedings of the National Academy of Sciences, 1987