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1 were extended with dATP by Escherichia coli DNA polymerase I.
2 not the Klenow fragment of Escherichia coli DNA polymerase I.
3 deficient large fragment of Escherichia coli DNA polymerase I.
4 ase-free Klenow fragment of Escherichia coli DNA polymerase I.
5 polymerase beta or Klenow fragment of E.coli DNA polymerase I.
6 eficient Klenow fragment of Escherichia coli DNA polymerase I.
7 ly in a crystal of the thermostable Bacillus DNA polymerase I.
8 th the equivalent region of Escherichia coli DNA polymerase I.
9 s, beta interacts with MutS, DNA ligase, and DNA polymerase I.
10 s by the Klenow fragment of Escherichia coli DNA polymerase I.
11 the proofreading domain of Escherichia coli DNA polymerase I.
12 (exo(-)) Klenow fragment of Escherichia coli DNA polymerase I.
13 exo-nuclease III and the Klenow fragment of DNA polymerase I.
14 atalytic site (motif A) of Thermus aquaticus DNA polymerase I.
15 oofreading by the Klenow fragment of E. coli DNA polymerase I.
16 reverse transcriptase, T7 DNA polymerase, or DNA polymerase I.
17 -3' exonuclease function of Escherichia coli DNA polymerase I.
18 e to restriction endonucleases, and notably, DNA polymerase I.
19 ge proteolytic fragment (Klenow fragment) of DNA polymerase I.
20 now fragment (KF exo-) from Escherichia coli DNA polymerase I.
21 prior work on the mechanism and dynamics of DNA polymerase I.
22 s and also by the Klenow fragment of E. coli DNA polymerase I.
23 sive sequence homology with Escherichia coli DNA polymerase I.
24 agment (KF, exo- mutant) of Escherichia coli DNA polymerase I.
25 gue, the Klenow fragment of Escherichia coli DNA polymerase I.
26 ly from the closely related Escherichia coli DNA polymerase I.
27 taricus Dpo4 and Bacillus stearothermophilus DNA polymerase I.
28 of palm domain containing proteins, such as DNA polymerase I.
29 ase-free Klenow fragment of Escherichia coli DNA polymerase I.
30 palm domains of phosphodiesterases, such as DNA polymerase I.
31 Arg(841) present in the fingers subdomain of DNA polymerase I.
35 FEN1 or the 5'-nuclease domains of bacterial DNA polymerases is a double-flap structure containing a
36 epair pathway requires the Vsr endonuclease, DNA polymerase I, a DNA ligase, MutS, and MutL to functi
37 ue of the small fragment of Escherichia coli DNA polymerase I, a FEN with which it shares 66% similar
38 elity of DNA replication by bacteriophage T4 DNA polymerase is achieved in a multiplicative process:
42 s less topo I was recruited, suggesting that DNA polymerase is an important modulator of the binding
43 DNA polymerase, a variant of the 9 degrees N DNA polymerase, is an efficient DNA-directed threosyl nu
46 e interaction between the Klenow fragment of DNA polymerase I and a series of defined oligonucleotide
47 ase active site motifs with Escherichia coli DNA polymerase I and bacteriophage T7 DNA polymerase.
48 the single strand break by endonuclease IV, DNA polymerase I and DNA ligase occurred and was not gre
50 nd break can be repaired by Escherichia coli DNA polymerase I and E. coli DNA ligase alone, though le
51 osite a single strand break, endonuclease IV DNA polymerase I and Escherichia coli DNA ligase are req
52 ve site and in different segments of E. coli DNA polymerase I and have determined the effects of thes
53 iously determined for the Klenow fragment of DNA polymerase I and is consistent with recent structura
54 and developed purification methods for whole DNA polymerase I and its 5'-3' exonuclease domain that a
55 A-binding proteins, the Klenow fragment from DNA polymerase I and Klenow exonuclease minus (which has
57 amers did not inhibit the Klenow fragment of DNA polymerase I and only had a minor effect on RB69 DNA
58 e interaction between the Klenow fragment of DNA polymerase I and synthetic DNA primer-templates cont
59 sive sequence homology with Escherichia coli DNA polymerase I and T7 DNA polymerase, it contains uniq
60 of nucleotide repeats during replication by DNA polymerase I and that this action provides insight i
61 the Klenow fragment of the Escherichia coli DNA polymerase I and the Bacillus stearothermophilus pol
62 instead required polA and polC, which encode DNA polymerase I and the second DNA polymerase III enzym
63 combine single-molecule FRET with the use of DNA polymerase I and various fidelity mutants to highlig
65 onucleases, especially those associated with DNA Polymerases I and III, affect inheritance of the sil
69 olymerization rate of the Klenow fragment of DNA polymerase I, and we demonstrate its combination wit
70 labeled using digoxigenin-11-dUTP and Klenow DNA polymerase-I, and detected using fluorescein isothio
71 I since very-long patch BER was inhibited by DNA polymerase I antibody and addition of excess DNA pol
72 m of the Klenow fragment of Escherichia coli DNA polymerase I as well as DNA polymerase of Thermus aq
73 small amounts of template by RCA using phi29 DNA polymerase is "background" DNA synthesis that usuall
74 tolerance to mutation in the active sites of DNA polymerases is being exploited to engineer polymeras
75 e or the Klenow fragment of Escherichia coli DNA polymerase I, both nucleotides failed to substitute
76 ort the crystal structure of a high fidelity DNA polymerase I bound to DNA primer-template caught in
77 bases can migrate through the run while the DNA polymerase is bound to the template-primer, or the D
78 ain of gp43 is homologous to that of E. coli DNA polymerase I but lies on the opposite side of the po
79 modification does not affect the activity of DNA polymerase I, but four vinylphosphonate linkages in
80 In prokaryotes, this process is completed by DNA polymerase I by means of strand displacement DNA syn
84 of DNA polymerse I in Escherichia coli, the DNA polymerase I class of enzymes has served as the prot
85 are presented for a Thermus aquaticus (Taq) DNA polymerase I complex (consisting of the protein, the
89 s relatives, our biochemical analysis of the DNA polymerase is consistent with the postulated nonther
90 We show that PolC is highly dynamic: this DNA polymerase is constantly recruited to and released f
91 ce present in the Mycobacterium tuberculosis DNA polymerase I corresponds to a hinge region in the fi
93 upled with the conformational transitions in DNA polymerases is critical for maintaining the fidelity
95 Klenow fragment (exo(-)) of Escherichia coli DNA polymerase I demonstrate that bypass of LdG modifica
96 ons with the 3'-5' exo(-) Klenow fragment of DNA polymerase I demonstrate the usefulness of our proto
97 Telomerase is the cellular RNA-dependent DNA polymerase (i.e. reverse transcriptase) that uses an
99 uctures provide the first direct evidence in DNA polymerase I enzymes of a large conformational chang
102 e chemical step in the catalytic reaction of DNA polymerases is essential for elucidating the molecul
103 catalytic subunit of the eukaryotic B-family DNA polymerases is essential for the formation of active
104 n of UL42 and BMRF1 with their corresponding DNA polymerases is essential for viral DNA replication a
107 cluding exonucleases I-IX (including the two DNA polymerase I exonucleases), RecJ exonuclease, SbcCD
108 ear antigen (PCNA), the auxiliary factor for DNA polymerase , is expressed zygotically in the develop
111 of dATP and dGTP analogues to determine how DNA polymerase I from Bacillus stearothermophilus (BF),
112 tensive studies using the Klenow fragment of DNA polymerase I from E. coli (Kf) and found to be recog
113 tic experiments using the Klenow fragment of DNA polymerase I from E. coli suggest that a low dA misi
116 eolytic active site of the large fragment of DNA polymerase I from Escherichia coli have been elucida
119 eal overdamped, coupled domain motion within DNA polymerase I from Thermus aquaticus (Taq polymerase)
121 substrate recognition in the active site of DNA polymerase I from Thermus aquaticus (Taq) and select
126 e binding established previously for several DNA polymerases is generally extended to all DNA polymer
127 onuclease activity of the Klenow fragment of DNA polymerase I has been investigated with a combinatio
129 nd cannot grow at moderate temperatures, its DNA polymerase I has significant activity at 20-37 degre
134 ulgidus and Methanococcus jannaschii and the DNA polymerase I homologues from Thermus aquaticus and T
135 The Klenow fragment of Escherichia coli DNA polymerase I houses catalytic centers for both polym
136 sly, it has been shown that Escherichia coli DNA polymerases I, II, and III are incapable of bypassin
139 propose a new in vivo function for wild-type DNA polymerase I in chromosome termination at site(s) no
140 t the crystal structure of Thermus aquaticus DNA polymerase I in complex with an inhibitory Fab, TP7,
141 the closed, open, and ajar conformations of DNA polymerase I in the binary (enzyme:DNA) state to bet
142 RNase D and the 3'-5' exonuclease domain of DNA polymerase I in the Werner syndrome gene product.
143 The Klenow exo- fragment of Escherichia coli DNA polymerase I incorporated 2'-deoxyadenosine (dA) six
144 Taq, the large fragment of Thermus aquaticus DNA polymerase I, incorporates a nucleotide opposite an
148 forks or suppress futile origin firing when DNA polymerase is inhibited, leading to incomplete genom
149 ts demonstrate that the COOH terminus of the DNA polymerase is inserted into the subunit interface of
150 g single molecules of the Klenow fragment of DNA polymerase I into electronic nanocircuits allowed el
151 a also suggest that an aphidicolin-sensitive DNA polymerase is involved in the excision step of the n
152 tein, a eukaryotic member of the Y family of DNA polymerases, is involved in the tolerance of DNA dam
153 e Stoffel fragment (SF) of Thermus aquaticus DNA polymerase I is displayed on a filamentous phage by
155 the thermodynamics of substrate selection by DNA polymerase I is important for characterizing the bal
158 to modulate DNA strand slippage synthesis by DNA polymerase I, is a wedge-shaped spirocyclic molecule
159 and previous observations that mitochondrial DNA polymerase is itself a reverse transcriptase, we pro
161 uses the Klenow fragment of Escherichia coli DNA polymerase I (KF) and fluorescently labeled primer/t
162 with the Klenow fragment of Escherichia coli DNA polymerase I (KF) as a function of the concentration
163 use the Klenow fragment of Escherichia coli DNA polymerase I (KF) as a model proofreading polymerase
164 and the Klenow fragment of Escherichia coli DNA polymerase I (KF) incorporate all four nucleotide an
165 nt burst synthesis rate for Escherichia coli DNA Polymerase I (KF) was found to be an order of magnit
168 sence of Klenow fragment of Escherichia coli DNA polymerase I (Kfexo(-)) and DNA polymerase beta (pol
174 In the same constructs, Escherichia coli DNA polymerase I Klenow Fragment exo(-) is much less eff
175 a much better substrate for the model enzyme DNA polymerase I Klenow fragment lacking proofreading ac
176 tilizing the Escherichia coli UvrD helicase, DNA polymerase I Klenow fragment, two accessory proteins
177 an indirect assay employing Escherichia coli DNA polymerase I (Klenow enzyme) and poly(dT) template.
178 he dissociation constants for the binding of DNA polymerase I (Klenow fragment) (KF) to the primer-te
179 r extension by exonuclease-deficient E. coli DNA polymerase I (Klenow fragment) (KF) when (+)-trans-
180 e insertion by exonuclease-deficient E. coli DNA polymerase I (Klenow fragment) across from either th
181 ite-specific mutagenesis of Escherichia coli DNA polymerase I (Klenow fragment) and atomic substituti
182 of an exonuclease-deficient Escherichia coli DNA polymerase I (Klenow fragment) bound to primer-templ
183 rboxylate ligands, Asp(705) and Asp(882), of DNA polymerase I (Klenow fragment) in the early prechemi
184 mechanism of bypass by the Escherichia coli DNA polymerase I (Klenow fragment) in the presence of th
185 In particular, Arg668 of Escherichia coli DNA polymerase I (Klenow fragment) makes a critical cont
186 fer, we observed individual Escherichia coli DNA polymerase I (Klenow fragment) molecules performing
187 approach to monitor the movement of E. coli DNA polymerase I (Klenow fragment) on a DNA template dur
188 ts show that the binding of Escherichia coli DNA polymerase I (Klenow fragment) to a primer-template
189 of an exonuclease-deficient Escherichia coli DNA polymerase I (Klenow fragment) to DNA primer-templat
191 he mutant sites of duplex DNA was induced by DNA polymerase I (Klenow fragment) to preserve Watson-Cr
192 hree active-site mutants of Escherichia coli DNA polymerase I (Klenow fragment) were used to study DN
193 nsition that occurs when a binary complex of DNA polymerase I (Klenow fragment) with a primer-templat
194 lymerase ternary complex of Escherichia coli DNA polymerase I (Klenow fragment), containing the templ
195 dG adducts, positioned in the active site of DNA polymerase I (Klenow fragment), serve as donor fluor
198 process were studied using Escherichia coli DNA polymerase I (Klenow fragment, 3'-exonuclease defici
200 s of the large fragment of Thermus aquaticus DNA polymerase I (Klentaq1) with a primer/template DNA a
203 polymerase beta, a member of the X family of DNA polymerases, is known to be involved in base excisio
205 NA polymerases were investigated: mesophilic DNA polymerase I large (Klenow) fragment, 3'-->5' exo(-)
206 se (TteUvrD) and Bacillus stearothermophilus DNA polymerase I Large Fragment (Bstpol) using a coiled-
207 Nt.CviPII was used in combination with Bst DNA polymerase I large fragment to rapidly amplify anony
208 ures and enzyme kinetic analyses of Bacillus DNA polymerase I large fragment variants complexed with
209 able bacterial (Bacillus stearothermophilus) DNA polymerase I large fragments with DNA primer templat
210 novel polymerase from the well characterized DNA polymerase I-like Thermus thermophilus DNA polymeras
215 Furthermore, we have found that the viral DNA polymerase is mislocalized to the cytoplasm in both
216 A mechanism by which the Klenow fragment of DNA polymerase I monitors the geometry of the base pairs
217 The polymerase and 5'-nuclease components of DNA polymerase I must collaborate in vivo so as to gener
219 f mutation rates, we generated a panel of 66 DNA polymerase I mutants in Escherichia coli with compar
220 al proof that the D(752) allele in the viral DNA polymerase is necessary and sufficient for expressio
221 ther the Klenow fragment of Escherichia coli DNA polymerase I nor the T7 DNA polymerase, both of whic
224 hich rat DNA polymerase beta substitutes for DNA polymerase I of Escherichia coli, we previously isol
227 d by the Klenow fragment of Escherichia coli DNA polymerase I or by calf thymus DNA polymerase alpha.
230 We demonstrated that the Klenow fragment (DNA polymerase I) performs translesion synthesis on this
231 The LEXE motif, conserved in eukaryotic type DNA polymerases, is placed close to the polymerization a
233 ts in the O-helix of Thermus aquaticus (Taq) DNA polymerase I (pol I) for altered fidelity of DNA syn
234 s ability to substitute for Escherichia coli DNA polymerase I (pol I) in the SC18-12 strain, which la
238 elity of DNA replication by Escherichia coli DNA polymerase I (pol I) was assessed in vivo using a re
239 irectly visualize single fluorescent labeled DNA polymerase I (Pol) and ligase (Lig) molecules search
240 he 'non-replicative' DNA polymerases, namely DNA polymerase I (polA), II (polB), IV (dinB) and V (umu
241 expressed from an operon encoding a putative DNA polymerase I (PolA1), among other GAS products.
242 ditionally, deletion of the Klenow domain of DNA polymerase I (PolI) resulted in a approximately 35-f
246 m that we previously deduced for Dpo4 and T7 DNA polymerases is preferred for Pol kappa as well, sugg
247 chanism for the observed expansions with Taq DNA polymerase is proposed that does not invoke strand s
251 support a model in which the leading strand DNA polymerase is recruited prior to origin DNA unwindin
252 the difference between low and high fidelity DNA polymerases is related to the efficiency of correct,
254 The Polzeta translesion synthesis (TLS) DNA polymerase is responsible for over 50% of spontaneou
255 ed primarily in the repair of DNA whereas T7 DNA polymerase is responsible for the replication of the
261 that the Klenow fragment of Escherichia coli DNA polymerase I stopped synthesis mostly after incorpor
262 termining the biochemical properties of this DNA polymerase is structure-function studies of site-spe
263 sive (homologous or heterologous) "trailing" DNA polymerase is sufficient to improve gp41 processivit
264 oding the catalytic subunit of mitochondrial DNA polymerase is sufficient to support physiological va
265 With the Klenow fragment of Escherichia coli DNA polymerase I, synthesis stops at the base immediatel
266 200,000 members) of mutant Thermus aquaticus DNA polymerase I (Taq pol I) was created containing rand
267 200,000 members) of mutant Thermus aquaticus DNA polymerase I (Taq pol I) was created containing rand
268 DNA polymerases including Thermus aquaticus DNA polymerase I (Taq Pol), a thermostable enzyme common
269 s in the Klenow fragment of Escherichia coli DNA polymerase I that interact with the ssDNA overhang o
271 sequence analyses suggest that the class II DNA polymerase is the principal DNA replicative enzyme o
272 e nucleotidyl transfer reaction catalyzed by DNA polymerases is the critical step governing the accur
273 beta (polbeta), a member of the X family of DNA polymerases, is the major polymerase in the base exc
274 not a member of the Y family of error-prone DNA polymerases, is the primary mediator of survival thr
275 ith four polymerases, the Klenow fragment of DNA polymerase I, the Klenow fragment with the proof-rea
276 ses (the Klenow fragment of Escherichia coli DNA polymerase I, the modified T7 DNA polymerase (Sequen
278 The Klenow fragment of Escherichia coli DNA polymerase I then elongates the template-primer by t
279 erase X (pol X), a member of the X family of DNA polymerases, is thought to be involved in base excis
280 distribution was influenced by the ratio of DNA polymerase I to DNA ligase activity in the reaction.
283 -slide application of the Klenow fragment of DNA polymerase I to extend unmodified miRNAs hybridized
284 ditionally, Cu(II) chelated PyED outcompetes DNA polymerase I to successfully inhibit template strand
285 he ability of the Klenow fragment of E. coli DNA polymerase I to synthesize and extend the different
286 ne POLG, coding for the catalytic subunit of DNA polymerase, is typically proximal with early ophthal
287 tor of translesion DNA synthesis because the DNA polymerase is unable to extend beyond the incorporat
289 appa (Polkappa), a member of the Y-family of DNA polymerases, is unable to insert nucleotides opposit
291 ' exonuclease free (exo-) Klenow fragment of DNA polymerase I was used, dG-N2-3MeE promoted mostly on
292 with the Klenow fragment of Escherichia coli DNA polymerase I, we find that DDI markedly enhances the
293 lease reaction catalyzed by Escherichia coli DNA polymerase I, we have constructed expression plasmid
294 ce of the J-helix region of Escherichia coli DNA polymerase I, we performed site-directed mutagenesis
295 Various polymerization conditions using DNA polymerase I were examined to determine optimal labe
296 A by the Klenow fragment of Escherichia coli DNA polymerase I when individually substituted for its n
297 d by the Klenow fragment of Escherichia coli DNA polymerase I with better efficiency and fidelity tha
299 fidelity Klenow fragment of Escherichia coli DNA polymerase I with the proofreading exonuclease activ
300 ween the Klenow fragment of Escherichia coli DNA polymerase I with the proofreading exonuclease inact
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