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1 ludes the nearby dinB+ gene (for error-prone DNA polymerase IV).
2 leted for the SOS gene dinB, which codes for DNA polymerase IV.
3 notype that is suppressed by inactivation of DNA polymerase IV.
4 ed was examined with Solfolobus solfataricus DNA polymerase IV, a member of the RAD30A subfamily of t
5                         E. coli dinB encodes DNA polymerase IV and greatly increases spontaneous muta
6  DNA polymerases, including Escherichia coli DNA polymerase IV and human DNA polymerase kappa, effici
7  stress-induced ampD mutations require DinB (DNA polymerase IV) and partially require error-prone DNA
8  repair system and the inducible error-prone DNA polymerase IV, and the mutations are mostly -1 delet
9 ing affinity is an intrinsic property of the DNA polymerase IV-beta clamp interaction and not an indi
10                                              DNA polymerase IV binds dNTP substrates with about 10-fo
11                                    Bypass by DNA polymerase IV came at the expense of the inherent le
12                           We show that DinB (DNA polymerase IV) catalyses accurate TLS over one such
13 primitive DNA damage checkpoint and prevents DNA polymerase IV-dependent -1 frameshift mutagenesis, w
14 strate that YqjH has 36% identity to E. coli DNA polymerase IV (DinB protein), and YqjW has 26% ident
15 t for cleavage and interacts physically with DNA polymerase IV (DinB) and the beta clamp.
16 rding the role of SOS-inducible, error-prone DNA polymerase IV (DinB) in spontaneous mutation are res
17  proteins, the SOS response, and error-prone DNA polymerase IV (DinB), amplification requires neither
18                   We show that the increased DNA polymerase IV-dNTP binding affinity is an intrinsic
19 tension studies have shown that the Y-family DNA polymerase IV (Dpo4) from Sulfolobus solfataricus P2
20                                     Y-Family DNA polymerase IV (Dpo4) from Sulfolobus solfataricus se
21 sfer reaction catalyzed by the lesion-bypass DNA polymerase IV (Dpo4) from Sulfolobus solfataricus, w
22                   Sulfolobus solfataricus P2 DNA polymerase IV (Dpo4) has been shown to catalyze bypa
23 imer extension by Sulfolobus solfataricus P2 DNA polymerase IV (Dpo4) indicated preferential incorpor
24     These data indicate that the error-prone DNA polymerase IV (Dpo4) inefficiently extended past the
25                   Sulfolobus solfataricus P2 DNA polymerase IV (Dpo4) is a DinB homolog that belongs
26                      Sulfolobus solfataricus DNA polymerase IV (Dpo4) is a member of the Y family of
27                   Sulfolobus solfataricus P2 DNA polymerase IV (Dpo4) is a thermostable archaeal enzy
28 tion catalyzed by Sulfolobus solfataricus P2 DNA polymerase IV (Dpo4) is resolved by pre-steady-state
29 merase kappa homolog Sulfolobus solfataricus DNA polymerase IV (Dpo4) produces "-1" frameshift deleti
30 cs with the Y-family Sulfolobus solfataricus DNA polymerase IV (Dpo4) showed 90-fold higher incorpora
31 family polymerase Sulfolobus solfataricus P2 DNA polymerase IV (Dpo4) using single-molecule fluoresce
32  lesion catalyzed by Sulfolobus solfataricus DNA polymerase IV (Dpo4), a model Y-family DNA polymeras
33 r pre-steady-state kinetic studies show that DNA polymerase IV (Dpo4), a prototype Y-family enzyme fr
34 , can be bypassed by Sulfolobus solfataricus DNA polymerase IV (Dpo4), although this representative Y
35 d, with the Y-family Sulfolobus solfataricus DNA polymerase IV (Dpo4), at resolutions between 2.4 and
36 mily DNA polymerase, Sulfolobus solfataricus DNA polymerase IV (Dpo4), for the correct insertion of d
37 N(2)-epsilondG by Sulfolobus solfataricus P2 DNA polymerase IV (Dpo4), leading to a one-base deletion
38 mily DNA polymerase, Sulfolobus solfataricus DNA polymerase IV (Dpo4).
39 ossesses a DinB homolog that has been termed DNA polymerase IV (Dpo4).
40                             Escherichia coli DNA polymerase IV encoded by the dinB gene is involved i
41                             Escherichia coli DNA polymerase IV, encoded by the dinB gene, is a member
42 eotide deletions is a biological hallmark of DNA polymerase IV infidelity responsible for enhancing c
43 anslesion synthesis polymerases tested, only DNA polymerase IV, not DNA polymerase II, could engage p
44          Our efforts to understand why DinB (DNA polymerase IV) overproduction is cytotoxic to Escher
45 ved Escherichia coli result from error-prone DNA polymerase IV (Pol IV) (DinB) and that the mutagenes
46 response sigma factor, regulates error-prone DNA polymerase IV (Pol IV) (encoded by the dinB gene).
47 e activity of the specialized DNA polymerase DNA polymerase IV (Pol IV) both in stationary-phase and
48                        SOS-induced levels of DNA polymerase IV (Pol IV) confer UV sensitivity upon th
49              The actions of Escherichia coli DNA Polymerase IV (Pol IV) in mutagenesis are managed by
50 oli strains with and without the error-prone DNA polymerase IV (Pol IV) were compared.
51                             Escherichia coli DNA polymerase IV (pol IV), a member of the error-prone
52 tion in FC40 mostly results from error-prone DNA polymerase IV (Pol IV), encoded by dinB; most of the
53  largely but not entirely due to error-prone DNA polymerase IV (Pol IV).
54 pair, Saccharomyces cerevisiae has only one, DNA polymerase IV (pol IV).
55 t strains had 1/10 the amount of error-prone DNA polymerase IV (Pol IV).
56 tly homologous with that of Escherichia coli DNA polymerase IV (pol IV).
57                             Escherichia coli DNA polymerase IV (Pol IV, also known as DinB) is a Y-fa
58                       Escherichia coli DinB (DNA polymerase IV) possesses an enzyme architecture resu
59                                    Bypass by DNA polymerase IV required its ability to interact with
60 erty for the beta clamp, which when bound to DNA polymerase IV results in a large increase in dNTP bi
61 irect consequence of an increased binding of DNA polymerase IV to DNA.
62 and thus prevents binding of the translesion DNA polymerase IV to the clamp, providing a novel insigh

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