Base-excision repair activity of uracil-DNA glycosylase monitored using the latch zone of α-hemolysin.
about
Detection of benzo[a]pyrene-guanine adducts in single-stranded DNA using the α-hemolysin nanoporeTemperature and electrolyte optimization of the α-hemolysin latch sensing zone for detection of base modification in double-stranded DNA.Single-molecule investigation of G-quadruplex folds of the human telomere sequence in a protein nanocavity.Effect of an Electrolyte Cation on Detecting DNA Damage with the Latch Constriction of α-Hemolysin.Single-molecule analysis of thymine dimer-containing G-quadruplexes formed from the human telomere sequence.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.Unzipping of A-Form DNA-RNA, A-Form DNA-PNA, and B-Form DNA-DNA in the α-Hemolysin Nanopore.Differentiation of G:C vs A:T and G:C vs G:mC Base Pairs in the Latch Zone of α-Hemolysin.Nanopore Sensing.Single pyrimidine discrimination during voltage-driven translocation of osmylated oligodeoxynucleotides via the α-hemolysin nanopore.Base Flipping within the α-Hemolysin Latch Allows Single-Molecule Identification of Mismatches in DNA.Contact bubble bilayers with flush drainage.Interrogation of Base Pairing of the Spiroiminodihydantoin Diastereomers Using the α-Hemolysin Latch.Kinetics of T3-DNA Ligase-Catalyzed Phosphodiester Bond Formation Measured Using the α-Hemolysin Nanopore.Energetics of base flipping at a DNA mismatch site confined at the latch constriction of α-hemolysin.Dynamics of a DNA Mismatch Site Held in Confinement Discriminate Epigenetic Modifications of Cytosine.
P2860
Q28558816-AF91E988-775C-4BD0-B0D1-9036761CFA9AQ34080057-55A3F4E9-5937-49DC-A38E-EAFBF3E81A69Q34407493-88E043C7-EB1B-4B94-8072-9DBBBDEA1182Q34481812-B1C6FE20-4AF8-419D-8FBB-4CB41E41A7BDQ34680164-5087F09F-1CDC-406B-925B-6F9D0952AFC0Q35885854-BC9A45F4-75BE-4A59-8C47-D0B7924608CDQ36495381-6114F3C8-C136-4E25-BE94-199DB5BD83A6Q36926219-7E6EC936-22C3-4AED-8102-3F55AA270A79Q39096249-332BA4F1-DDA4-42AA-8439-E59CCAE0DD1AQ39960932-79B207F1-7F6B-4F8B-AA75-9B0CDCE65331Q40077513-80053654-D31F-4AB4-B5FE-3F204D1019E4Q43187253-DE353997-9CB1-4D02-9DED-AFEF7C99C624Q46413562-19578336-26F9-492D-9DFF-C0891CDBC546Q47135405-4768B448-41B1-4521-AD8C-2842A76055DEQ47164833-F85DEA19-41C5-4858-A653-16EBF75A3D44Q48308502-62318EB1-B2CA-415D-934B-B267E5AF06B9
P2860
Base-excision repair activity of uracil-DNA glycosylase monitored using the latch zone of α-hemolysin.
description
article científic
@ca
article scientifique
@fr
articolo scientifico
@it
artigo científico
@pt
bilimsel makale
@tr
scientific article published on 11 December 2013
@en
vedecký článok
@sk
vetenskaplig artikel
@sv
videnskabelig artikel
@da
vědecký článek
@cs
name
Base-excision repair activity ...... the latch zone of α-hemolysin.
@en
Base-excision repair activity ...... the latch zone of α-hemolysin.
@nl
type
label
Base-excision repair activity ...... the latch zone of α-hemolysin.
@en
Base-excision repair activity ...... the latch zone of α-hemolysin.
@nl
prefLabel
Base-excision repair activity ...... the latch zone of α-hemolysin.
@en
Base-excision repair activity ...... the latch zone of α-hemolysin.
@nl
P2093
P2860
P356
P1476
Base-excision repair activity ...... the latch zone of α-hemolysin.
@en
P2093
Aaron M Fleming
Cynthia J Burrows
Henry S White
P2860
P304
19347-19353
P356
10.1021/JA410615D
P407
P577
2013-12-11T00:00:00Z