Fluorescent Single-Stranded DNA Binding Protein as a Probe for Sensitive, Real-Time Assays of Helicase Activity: Biophysical Journal
Por um escritor misterioso
Last updated 11 maio 2024
PDF] Fluorescence stopped-flow studies of single turnover kinetics of E.coli RecBCD helicase-catalyzed DNA unwinding.
Frontiers Approaching Protein Barriers: Emerging Mechanisms of Replication Pausing in Eukaryotes
Phase separation by ssDNA binding protein controlled via protein−protein and protein−DNA interactions
Deciphering the mechanism of processive ssDNA digestion by the Dna2-RPA ensemble
PcrA Helicase Tightly Couples ATP Hydrolysis to Unwinding Double-Stranded DNA, Modulated by the Initiator Protein for Plasmid Replication, RepD
Molecular Microbiology, Microbiology Journal
Fluorescent Single-Stranded DNA Binding Protein as a Probe for Sensitive, Real-Time Assays of Helicase Activity: Biophysical Journal
The HRDC domain of E. coli RecQ helicase controls single-stranded DNA translocation and double-stranded DNA unwinding rates without affecting mechanoenzymatic coupling
Applied Nano, Free Full-Text
Helicase Activity Modulation with On-Demand Light-Based Conformational Control
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