21 results on '"Jergic, Slobodan"'
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2. Mechanism of transcription modulation by the transcription-repair coupling factor
3. DnaB helicase dynamics in bacterial DNA replication resolved by single-molecule studies
4. Proofreading exonuclease on a tether: the complex between the E. coli DNA polymerase III subunits α, ϵ, θ and β reveals a highly flexible arrangement of the proofreading domain
5. Single-molecule live-cell imaging reveals RecB-dependent function of DNA polymerase IV in double strand break repair
6. Development of a single-stranded DNA-binding protein fluorescent fusion toolbox
7. Real-time single-molecule observation of rolling-circle DNA replication
8. The proofreading exonuclease subunit ϵ of Escherichia coli DNA polymerase III is tethered to the polymerase subunit α via a flexible linker
9. The unstructured C-terminus of the τ subunit of Escherichia coli DNA polymerase III holoenzyme is the site of interaction with the α subunit
10. Solution structure of Domains IVa and V of the τ subunit of Escherichia coli DNA polymerase III and interaction with the α subunit
11. Recycling of single-stranded DNA-binding protein by the bacterial replisome
12. Exchange betweenEscherichia colipolymerases II and III on a processivity clamp
13. Two mechanisms coordinate replication termination by theEscherichia coliTus–Tercomplex
14. Proofreading exonuclease on a tether: the complex between the E. coli DNA polymerase III subunits α, ε, θ and β reveals a highly flexible arrangement of the proofreading domain
15. Exchange between Escherichia coli polymerases II and III on a processivity clamp.
16. The proofreading exonuclease subunit ε of Escherichia coli DNA polymerase III is tethered to the polymerase subunit α via a flexible linker
17. Two mechanisms coordinate replication termination by the Escherichia coli Tus-Ter complex.
18. Proofreading exonuclease on a tether: the complex between the E. coli DNA polymerase III subunits α, ɛ, θ and β reveals a highly flexible arrangement of the proofreading domain.
19. The proofreading exonuclease subunit epsilon of Escherichia coli DNA polymerase III is tethered to the polymerase subunit alpha via a flexible linker.
20. Solution structure of Domains IVa and V of the tau subunit of Escherichia coli DNA polymerase III and interaction with the alpha subunit.
21. The unstructured C-terminus of the tau subunit of Escherichia coli DNA polymerase III holoenzyme is the site of interaction with the alpha subunit.
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