ArticleJournal of the American Chemical Society2013
Base-excision repair activity of uracil-DNA glycosylase monitored using the latch zone of α-hemolysin.
Article in Journal of the American Chemical Society, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.
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Who cites it
27 citing papers in PubMed, 57 citations in OpenAlex.
- Stochasticity in Single-Entity Electrochemistry.Current opinion in electrochemistry · 2021Article
- Analytical and Structural Studies for the Investigation of Oxidative Stress in Guanine Oligonucleotides.International journal of molecular sciences · 2020Review
- Direct Quantification of Damaged Nucleotides in Oligonucleotides Using an Aerolysin Single Molecule Interface.ACS central science · 2020Article
- Nanopore device-based fingerprinting of RNA oligos and microRNAs enhanced with an Osmium tag.Scientific reports · 2019Article
- Single-Molecule Protein Detection in a Biofluid Using a Quantitative Nanopore Sensor.ACS sensors · 2019Article
- γ-Hemolysin Nanopore Is Sensitive to Guanine-to-Inosine Substitutions in Double-Stranded DNA at the Single-Molecule Level.Journal of the American Chemical Society · 2018Article
- Nanoscale electrochemical kinetics & dynamics: the challenges and opportunities of single-entity measurements.Faraday discussions · 2018Article
- Mapping the sensing spots of aerolysin for single oligonucleotides analysis.Nature communications · 2018Article
- Single-Molecule Titration in a Protein Nanoreactor Reveals the Protonation/Deprotonation Mechanism of a C:C Mismatch in DNA.Journal of the American Chemical Society · 2018Article
- Nanopore Analysis of the 5-Guanidinohydantoin to Iminoallantoin Isomerization in Duplex DNA.The Journal of organic chemistry · 2018Article
- Interrogation of Base Pairing of the Spiroiminodihydantoin Diastereomers Using the α-Hemolysin Latch.Biochemistry · 2017Article
- Dynamics of a DNA Mismatch Site Held in Confinement Discriminate Epigenetic Modifications of Cytosine.Journal of the American Chemical Society · 2017Article
- Nanopore Sensing.Analytical chemistry · 2017Review
- Kinetics of T3-DNA Ligase-Catalyzed Phosphodiester Bond Formation Measured Using the α-Hemolysin Nanopore.ACS nano · 2016Article
- Energetics of base flipping at a DNA mismatch site confined at the latch constriction of α-hemolysin.Faraday discussions · 2016Article
- Base Flipping within the α-Hemolysin Latch Allows Single-Molecule Identification of Mismatches in DNA.Journal of the American Chemical Society · 2016Article
- Unzipping of A-Form DNA-RNA, A-Form DNA-PNA, and B-Form DNA-DNA in the α-Hemolysin Nanopore.Biophysical journal · 2016Article
- Single pyrimidine discrimination during voltage-driven translocation of osmylated oligodeoxynucleotides via the α-hemolysin nanopore.Beilstein journal of nanotechnology · 2016Article
- Differentiation of G:C vs A:T and G:C vs G:mC Base Pairs in the Latch Zone of α-Hemolysin.ACS nano · 2015Article
- Unfolding Kinetics of the Human Telomere i-Motif Under a 10 pN Force Imposed by the α-Hemolysin Nanopore Identify Transient Folded-State Lifetimes at Physiological pH.Journal of the American Chemical Society · 2015Article
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
Abstract
Nanopores have been investigated as a simple and label-free tool to characterize DNA nucleotides when a ssDNA strand translocates through the constriction of the pore. Here, a wild-type α-hemolysin protein nanopore was used to monitor DNA repair enzyme activity based on base-specific interactions of dsDNA with the vestibule constriction "latch", a previously unrecognized sensing zone in α-hemolysin specific for dsDNA structure. The presence of a single abasic site within dsDNA that is in proximity to the latch zone (±2 nucleotides) results in a large increase in ion channel current, allowing accurate quantitation of the kinetics of base repair reactions involving an abasic site product. Taking advantage of the high resolution for abasic site recognition, the rate of uracil-DNA glycosylase hydrolysis of the N-glycosidic bond, converting 2'-deoxyuridine in DNA to an abasic site, was continuously monitored by electrophoretically capturing reaction substrate or product dsDNA in the ion channel vestibule. Our work suggests use of the nanopore as an enzymology tool and provides a means to identify single base structural changes in dsDNA.
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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.