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1 foci post-UV that do not colocalize with the DnaB helicase.
2  be on the correct side of the helix to load DnaB helicase.
3 nable to block T7 RNA polymerase and E. coli DnaB helicase.
4 mobilized when each forms a complex with the DnaB helicase.
5 winding the DNA and promoting the binding of DnaB helicase.
6  the possible domain that interacts with the DnaB helicase.
7 d DNA (ssDNA) by the DnaB x DnaC complex and DnaB helicase.
8 gomeric structure, which is required to load DnaB helicase.
9  is similar to the intrinsic affinity of the DnaB helicase.
10  structure is insufficient by itself to load DnaB helicase.
11 is located on the large 33 kDa domain of the DnaB helicase.
12 y suppressing unproductive ATP hydrolysis by DnaB helicase.
13 atly stimulated through its interaction with DnaB helicase.
14                                              DnaB helicase accelerated the rate of primer syntheisis,
15 lts for a mechanistic model of the hexameric DnaB helicase action is discussed.
16 nd opening appeared normal but the levels of DnaB helicase activity were substantially reduced.
17 y further evaluation in a specific assay for DnaB helicase activity.
18                           In the presence of DnaB helicase, all trinucleotides could serve as the pri
19 how that the analogous Escherichia coli (Ec) DnaB helicase also interacts specifically with the exclu
20        Besides stimulating primase activity, DnaB helicase also prevented primase from synthesizing R
21 f crossing over were increased by defects in DnaB helicase and by oxidative damage, showing that dama
22 l protein system, composed solely of E. coli DnaB helicase and DNA polymerase III holoenzyme.
23  following inactivation of a thermosensitive DnaB helicase and found that they are distinct from thos
24 II) and polymerase IV (Pol IV) function with DnaB helicase and regulate its rate of unwinding, slowin
25 rrested Escherichia coli DNA replication and DnaB helicase and T7 RNA polymerase in vitro in both ori
26 in Escherichia coli requires the replicative DnaB helicase and the DNA primase, the DnaG gene product
27                      The complex between the DnaB helicase and the DnaG primase unwinds duplex DNA at
28 r complex physically interacts with both the DnaB helicase and the polymerase III (Pol III) core alph
29 ommon to known replicative helicases such as DnaB helicase and the SV40 T-antigen.
30 gruencies between the CMG and both bacterial DnaB helicases and the AAA+ motor of the eukaryotic prot
31  interaction between wild type pi with DnaA, DnaB helicase, and DnaG primase on one hand and between
32  priming reaction by employing DnaG primase, DnaB helicase, and ribonucleotidetriphosphates (incorpor
33  plasmid DNA replication, as measured by the DnaB helicase- and gyrase-dependent formation of FI*, a
34 tion with initiator proteins, interestingly, DnaB helicase appears to have at least a limited number
35  the DnaC molecules, in the complex with the DnaB helicase, are induced by the binding to the helicas
36                             In contrast, the DnaB helicase associates stably with the replication for
37        A step that follows is the binding of DnaB helicase at oriC so that it is properly positioned
38 complex then forms, involving the binding of DnaB helicase at oriC so that it is properly positioned
39  for self-oligomerization and the loading of DnaB helicase at oriC, we asked if these functions are s
40               An AAA+ ATPase, DnaC, delivers DnaB helicase at the E. coli chromosomal origin by a poo
41 that utilizes ATP hydrolysis to assemble the DnaB helicase at the origin.
42 uiting and positioning an active form of the DnaB helicase at the RK2 replication origin by a DnaA-in
43 aining 14, or less, nucleotide residues, the DnaB helicase becomes a completely distributive enzyme.
44  the ATP nonhydrolyzable analog AMP-PNP, the DnaB helicase binds polymer DNA with a site-size of 20 +
45 experiments provide direct evidence that the DnaB helicase binds the 5' arm of the fork in a single o
46                  Moreover, unlike the E.coli DnaB helicase, both Pseudomonas helicases could be deliv
47                                              DnaB helicase bound ssDNA with a high affinity [Kd = (5.
48 P is necessary to engage the 3' arm with the DnaB helicase, but it does not change the initial distri
49  of enzymatic activities of Escherichia coli DnaB helicase by homologous and heterologous single-stra
50                      The acceleration of the DnaB helicase can be observed in the absence of primase,
51                                     Although DnaB helicase can unwind a variety of DNA substrates pos
52 h protein components of the Escherichia coli DnaB helicase complex with the replication factor, the D
53         Site-specific Trp --> Cys mutants of DnaB helicase demonstrated that conformational change up
54         The conformational transition of the DnaB helicase-DNA complex, preceding the unwinding, is a
55                                      Anthrax DnaB helicase (DnaB(BA)) is a 453-amino-acid, 50-kDa pol
56                By contrast, Escherichia coli DnaB helicase (DnaB(EC)) did not stimulate DnaG(BA) and
57 nce of the results in the functioning of the DnaB helicase-DnaC protein complex is discussed.
58 nd NTP-binding sites of the Escherichia coli DnaB helicase engaged in the DnaB-DnaC complex and the m
59 quence motifs that are characteristic of the DnaB helicase family.
60        Our results also showed a decrease of DnaB helicase foci per cell after UV, consistent with th
61 the ATP nonhydrolyzable analog, AMP-PNP, the DnaB helicase fully preserves its hexameric structure.
62 )uridine-5'-diphosphate) have shown that the DnaB helicase has a preference for purine nucleotides.
63 coli replication factor DnaC protein and the DnaB helicase have been performed using sedimentation ve
64 ggest that primarily a single subunit of the DnaB helicase hexamer is in contact with the DNA.
65 coefficient s20,w = 10.5 +/- 0.2 of the free DnaB helicase hexamer.
66                 The kinetic step-size of the DnaB helicase, i.e. the number of the base-pairs unwound
67              In vitro, the sequence arrested DnaB helicase in both orientations, albeit more weakly t
68  mechanistic model of the functioning of the DnaB helicase in DNA replication is discussed.
69                Upon addition of DnaC and the DnaB helicase in the presence of ATPgammaS, helicase is
70 f Escherichia coli physically interacts with DnaB helicase in vivo.
71 vitro by SV40 T antigen and Escherichia coli dnaB helicases in an orientation-independent manner.
72  required for recruitment of the Pseudomonas DnaB helicases in the initiation of RK2 replication.
73 e mechanism of the nucleotide binding to the DnaB helicase indicates the lack of the existence of a k
74                          The analysis of the DnaB helicase interactions with nonfluorescent, unmodifi
75 ese data suggest that the oligomerization of DnaB helicase involves at least two distinct protein-pro
76                                              DnaB helicase is a ring-shaped hexamer of 300 kDa that i
77                                              DnaB helicase is a ring-shaped hexamer that unwinds DNA
78 of the DNA polymerase III holoenzyme and the DnaB helicase is critical for coupling the replicase and
79 anism of the free energy transduction by the DnaB helicase is discussed.
80 anism of the free energy transduction of the DnaB helicase is discussed.
81  of these results for the functioning of the DnaB helicase is discussed.
82 onstrated that ssDNA binding activity of the DnaB helicase is necessary for directing the primase to
83 in the DNA polymerase III holoenzyme and the DnaB helicase is required for replication fork propagati
84                                              DnaB helicase is responsible for unwinding duplex DNA du
85  well as in loading DnaB onto the ssDNA than DnaB helicase itself.
86 he stimulation of open complex formation and DnaB helicase loading on oriV, even in the absence of th
87  other conserved residues leads to decreased DnaB helicase loading onto SSB-bound DNA.
88  vitro, for localized strand opening and for DnaB helicase mediated unwinding.
89  that the major conformational change of the DnaB helicase-nucleotide complex occurs in the formation
90 fication and is an intrinsic property of the DnaB helicase-nucleotide system.
91 f helicase A appears to have homology to the DnaB helicase of E. coli (approximately 25%).
92                                              DnaB helicase of E. coli unwinds duplex DNA in the repli
93 es of two other hexameric DNA helicases: the DnaB helicase of Escherichia coli and the T-antigen heli
94 diated by the C-terminal domain gamma of the DnaB helicase of Escherichia coli.
95  of three distinct structural domains of the DnaB helicase of Escherichia coli: domain alpha, amino a
96 at had lost the ability to bind and load the DnaB helicase of P. aeruginosa or Pseudomonas putida ont
97 s predominantly unaffected in the absence of DnaB helicase on short ssDNA templates, whereas in conju
98                                The effect of DnaB helicase on the initiation specificity of primase w
99 cation restart, reloading of the replicative DnaB helicase onto an abandoned replication fork.
100                               DnaC loads the DnaB helicase onto DNA as a prelude for primosome assemb
101 itment and correct spatial deposition of the DnaB helicase onto origins.
102 s capacity to mediate efficient reloading of DnaB helicase onto rolling circle replication products,
103 ate the transfer of one or more molecules of DnaB helicase onto the chromosome; the transferred DnaB,
104       In this report, we determined that one DnaB helicase or one DnaB-DnaC complex is bound to a sin
105                           The specificity of DnaB helicase places it on the lagging strand template w
106 DnaC, an archetypal loader for the bacterial DnaB helicase, play distinct roles in helicase loading a
107 nonhydrolyzable analog, AMP-PNP, the E. coli DnaB helicase preferentially binds to the 5' arm of the
108                            In the absence of DnaB helicase, primase preferentially primed the d(CTG)
109 m excludes conformational transitions of the DnaB helicase prior to ATP binding.
110 a helicase substrate, the ATPase activity of DnaB helicase remained uninhibited.
111  Secondary structural predictions of 4A' and DnaB helicases resemble the known structures of RecA and
112 acteriophage T7 gene 4 protein and bacterial DnaB helicase, respectively.
113               Binding of oligonucleotides to DnaB helicase resulted in a significant attenuation of t
114 e lagging strand, such as primase binding to DnaB helicase, RNA synthesis, and SS B antigen (SSB) dis
115                            It was shown that DnaB helicase stabilized the open or single-stranded con
116                                              DnaB helicase stimulated the second-order RNA primer syn
117                                    In vitro, DnaB helicase stimulates primase to synthesize primers o
118 tifiable structural/conformational states of DnaB helicase that are likely important in the helicase
119                           In the presence of DnaB helicase, the initiation preference was not only al
120                            In the absence of DnaB helicase, the majority of primers synthesized by pr
121 ssDNA templates, whereas in conjunction with DnaB helicase, the specificity was altered and this alte
122 the replication terminator protein (RTP) and DnaB helicase, there has been continuing debate in the l
123      This template length is the same as the DnaB helicase thermodynamic binding site size.
124 necessary to determine the optimal amount of DnaB helicase to achieve this stimulation because helica
125 eplicase on the beta-clamp and function with DnaB helicase to form alternative replisomes, even befor
126 erial DNA replication, DnaA protein recruits DnaB helicase to the chromosomal origin, oriC, leading t
127 ng it to the binding of the Escherichia coli DnaB helicase to unmodified, nonfluorescent single-stran
128 epsilonA)19, s20,w = 12.4, suggests that the DnaB helicase undergoes further conformational changes u
129                    The ring-shaped hexameric DnaB helicase unwinds duplex DNA at the replication fork
130                                    Thus, the DnaB helicase unzips the dsDNA in a reverse process to t
131 gging strand polymerases are tethered to the DnaB helicase via dimeric tau.
132                          Binding of ssDNA to DnaB helicase was significantly modulated by nucleotide
133 of long-range allosteric interactions in the DnaB helicase which encompass the entire DnaB hexamer.
134 been performed with the fluorescein-modified DnaB helicase, which allows an exclusive monitoring of t
135                           Association of the DnaB helicase with nucleotide cofactors is characterized
136                           Association of the DnaB helicase with the 20-mer is characterized by three
137 ted by TrfA result in a repositioning of the DnaB helicase within the open origin region and an activ

 
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