ArticleNucleic acids research2010
Streamlined determination of processive run length and mechanochemical coupling of nucleic acid motor activities.
Article in Nucleic acids research, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
What it found
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Who cites it
8 citing papers in PubMed, 12 citations in OpenAlex.
- UPF1 mutants with intact ATPase but deficient helicase activities promote efficient nonsense-mediated mRNA decay.Nucleic acids research · 2022Article
- Intrinsically Disordered Linkers Impart Processivity on Enzymes by Spatial Confinement of Binding Domains.International journal of molecular sciences · 2019Article
- Shuttling along DNA and directed processing of D-loops by RecQ helicase support quality control of homologous recombination.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- The HRDC domain of E. coli RecQ helicase controls single-stranded DNA translocation and double-stranded DNA unwinding rates without affecting mechanoenzymatic coupling.Scientific reports · 2015Article
- Single-molecule motility: statistical analysis and the effects of track length on quantification of processive motion.Biophysical journal · 2013Article
- RecQ helicase translocates along single-stranded DNA with a moderate processivity and tight mechanochemical coupling.Proceedings of the National Academy of Sciences of the United States of America · 2012Article
- Complex activities of the human Bloom's syndrome helicase are encoded in a core region comprising the RecA and Zn-binding domains.Nucleic acids research · 2012Article
- Processive translocation mechanism of the human Bloom's syndrome helicase along single-stranded DNA.Nucleic acids research · 2010Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Quantitative determination of enzymatic rates, processivity and mechanochemical coupling is a key aspect in characterizing nucleotide triphosphate (NTP)-driven nucleic acid motor enzymes, for both basic research and technological applications. Here, we present a streamlined analytical method suitable for the determination of all key functional parameters based on measurement of NTP hydrolysis during interaction of motor enzymes with the nucleic acid track. The proposed method utilizes features of kinetic time courses of NTP hydrolysis that have not been addressed in previous analyses, and also accounts for the effect of protein traps used in kinetic experiments on processivity. This analysis is suitable for rapid and precise assessment of the effects of mutations, physical conditions, binding partners and other effectors on the functioning of translocases, helicases, polymerases and other NTP-consuming processive nucleic acid motors.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.