- Impact of macromolecular crowding on DNA replication. 2013
- An interaction between DNA polymerase and helicase is essential for the high processivity of the bacteriophage T7 replisome.
- Binding of Mn-deoxyribonucleoside triphosphates to the active site of the DNA polymerase of bacteriophage T7.
- Conformational dynamics of bacteriophage T7 DNA polymerase and its processivity factor, Escherichia coli thioredoxin.
- DNA recognition by the DNA primase of bacteriophage T7: a structure-function study of the zinc-binding domain.
- Identification of DNA primase inhibitors via a combined fragment-based and virtual screening.
- Molecular crowding enhanced ATPase activity of the RNA helicase eIF4A correlates with compaction of its quaternary structure and association with eIF4G.
- Pyrovanadolysis, a pyrophosphorolysis-like reaction mediated by pyrovanadate, Mn2+, and DNA polymerase of bacteriophage T7.
- Thioredoxin, the processivity factor, sequesters an exposed cysteine in the thumb domain of bacteriophage T7 DNA polymerase.
- Zinc-binding domain of the bacteriophage T7 DNA primase modulates binding to the DNA template.