On the thermodynamics and kinetics of the cooperative binding of bacteriophage T4-coded gene 32 (helix destabilizing) protein to nucleic acid lattices
Author:
Publisher
Elsevier BV
Subject
Biophysics
Cited by 47 articles. 订阅此论文施引文献 订阅此论文施引文献,注册后可以免费订阅5篇论文的施引文献,订阅后可以查看论文全部施引文献
1. Regulation of T7 gp2.5 binding dynamics by its C-terminal tail, template conformation and sequence;Nucleic Acids Research;2023-05-31
2. Insight into the biochemical mechanism of DNA helicases provided by bulk-phase and single-molecule assays;Methods;2021-12
3. Mapping DNA conformations and interactions within the binding cleft of bacteriophage T4 single-stranded DNA binding protein (gp32) at single nucleotide resolution;Nucleic Acids Research;2020-12-24
4. Using microsecond single-molecule FRET to determine the assembly pathways of T4 ssDNA binding protein onto model DNA replication forks;Proceedings of the National Academy of Sciences;2017-04-17
5. A mathematical model of recombinase polymerase amplification under continuously stirred conditions;Biochemical Engineering Journal;2016-08
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