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1 These ends are susceptible to degradation by exonuclease I.
2 the 5'-to-3' activity of MutSalpha-activated exonuclease I.
3 NA results in protection from degradation by exonuclease I.
4 recently determined structure of the E. coli Exonuclease I.
5 ereas SCE-associated events are sensitive to exonuclease I.
6 ilar to the processive exonucleases RecJ and exonuclease I.
8 p of a mismatch, the net contribution of the exonuclease is a function of multiple opportunities to c
15 ly identified SSB-Ct binding site on E. coli exonuclease I, although the SSB binding domains in the t
18 etected the activities of two model enzymes, exonuclease I and uracil DNA glycosylase with high sensi
19 A 3' ends from resection by Escherichia coli exonucleases I and III and from end-healing by T4 polynu
20 ading strand bias was lost in the absence of exonucleases I and VII, suggesting that it results from
21 s dramatically stimulated by inactivation of exonucleases I and VII, which degrade single-strand DNA
24 mplicated RecJ exonuclease, exonuclease VII, exonuclease I, and exonuclease X in Escherichia coli met
27 Electrical force applied to individual ssDNA-exonuclease I complexes pulls the two molecules apart, w
31 ing subunit of the replisome, the varepsilon exonuclease, is essential for high-fidelity DNA replicat
32 tif, which, by analogy to other proofreading exonucleases, is essential for the catalytic activity.
33 to CCC DNA conversion, two 3' exonucleases, exonuclease I (Exo I) and Exo III, were used in combinat
35 escent probe system that shows resistance to exonuclease I (Exo I) digestion upon binding to ATP mole
36 elective detection of streptomycin, based on exonuclease I (Exo I), complimentary strand of aptamer (
41 lepsilon mutants that in combination with an exonuclease I (exo1) mutation could cause a synergistic
45 exes formed between Escherichia coli SSB and Exonuclease I (ExoI), a well-studied SSB-interacting enz
46 xperiments have implicated RecJ exonuclease, Exonuclease I (ExoI), and Exonuclease VII (ExoVII) in th
50 pose a model in which processivity of lambda exonuclease is expressed as the net result of competitio
51 recombinant MP90 and recombinant RNA editing exonuclease I from L. major, and recombinant RNA editing
52 of DNA polymerase-associated proofreading 3'-exonucleases is generally enhanced in less stable DNA re
53 nt in RecJ exonuclease, exonuclease VII, and exonuclease I, grow poorly in the presence of the base a
57 ition between elongating pol II and the Xrn2 exonuclease is integral to termination of transcription
59 no major defect in meiosis, suggesting that exonuclease I is unlikely to be the primary activity tha
60 coli there are 14 DNA exonucleases including exonucleases I-IX (including the two DNA polymerase I ex
62 berberine, is digested upon the addition of exonuclease I, leading to the release of berberine into
64 servation suggests that RecJ exonuclease and exonuclease I may enhance recombination by degrading the
69 in those instances where the proofreading 3'-exonuclease is not part of the polymerase polypeptide.
70 the 3' exonuclease of DNA polymerase III and exonuclease I on deletion via these mechanisms in vivo.
72 ; bacteriophage T4 dexA and Escherichia coli exonuclease I, processive 3'-->5' exodeoxyribonucleases
73 sed to measure the degradation of DNA by DNA exonuclease I, providing data that would not be availabl
74 ally, lowering deamination density increases exonuclease I recruitment and single-stranded DNA at the
79 n different biological matrices show that 5'-exonuclease is the most prevalent nuclease activity in e
80 , encoding the major mammalian 3' --> 5' DNA exonuclease, is the AGS1 gene, and AGS-causing mutations
83 d measured the time required by molecules of Exonuclease I to hydrolyze single-stranded DNA that was
84 ble method that utilizes exonuclease III and exonuclease I to interrogate the binding properties of s
85 hole observed in the crystal structure of T5 exonuclease is too small to permit the passage of double
86 The single-stranded DNA produced by lambda exonuclease is utilized by homologous pairing proteins t