コーパス検索結果 (1語後でソート)
通し番号をクリックするとPubMedの該当ページを表示します
1 e delta but instead depends, in part, on the thymine DNA glycosylase.
2 80-fold effects were observed previously for thymine DNA glycosylase.
3 same as reported for the human G/T mismatch thymine-DNA glycosylase.
4 mination product of 5hmC could be excised by thymine DNA glycosylase and MBD4 glycosylases regardless
6 rvation was paralleled by a compromised TDG (thymine DNA glycosylase) and TET1 (ten-eleven translocat
7 CadC, and 5-HmdU, may be cleaved from DNA by thymine DNA glycosylase, and subsequent action of base-e
8 ty differences between E. coli MUG and human thymine DNA glycosylase as well as that between the wild
9 the removal of thymine from a G.T mismatch, thymine DNA glycosylase binds tightly to the apurinic si
13 regeneration-associated genes in a Tet3- and thymine DNA glycosylase-dependent fashion in DRG neurons
17 cantly increases the rate of dissociation of thymine DNA glycosylase from apurinic sites, presumably
18 nesium does not increase the dissociation of thymine DNA glycosylase from G.AP sites sufficiently to
26 rted nucleobase excision activities of human thymine DNA glycosylase (hTDG) toward duplex DNA substra
27 ipping assay to study damage search by human thymine DNA glycosylase (hTDG), which initiates BER of m
29 s not influenced by either UNG1/2, SMUG1, or thymine-DNA glycosylase knockdown, strongly suggesting t
31 t pol beta, in concert with the T:G-specific thymine DNA glycosylase, may be intricately involved in
33 o 5-carboxylcytosine followed by excision by thymine-DNA glycosylase, raises the possibility that act
35 is lesion is repaired by a mismatch-specific thymine DNA glycosylase (TDG or G/T glycosylase), which
36 viously that the base excision repair enzyme thymine DNA glycosylase (TDG) acts as a potent coactivat
38 a 2'-fluoroarabino-substituted nucleotide by thymine DNA glycosylase (TDG) can be directly monitored
39 easoned that the base excision repair enzyme thymine DNA glycosylase (TDG) could be such a target for
41 lcytosine (fC), and 5-carboxycytosine (caC), thymine DNA glycosylase (TDG) excises fC or caC, and bas
46 aC), with 5fC and 5caC subject to removal by thymine DNA glycosylase (TDG) in conjunction with base e
47 nd T:G mispair, and this step is followed by thymine DNA glycosylase (TDG) initiated base excision re
54 alytic inactivation of the DNA repair enzyme thymine DNA glycosylase (TDG) leads to embryonic lethali
56 slocation (TET) enzymes (TET1/TET2/TET3) and thymine DNA glycosylase (TDG) play crucial roles in earl
62 ated cytosine, are recognized and removed by thymine DNA glycosylase (TDG) to generate an abasic site
63 g a panel of DNA demethylases, we found that thymine DNA glycosylase (TDG) up-regulated Wnt signaling
64 relationship between chromatin structure and thymine DNA glycosylase (TDG) using chemically defined n
66 air, we characterized oxoA excision by human thymine DNA glycosylase (TDG), an enzyme known to remove
68 oxylcytosine (caC), excision of fC or caC by thymine DNA glycosylase (TDG), and restoration of cytosi
69 oxylcytosine (caC), excision of fC or caC by thymine DNA glycosylase (TDG), and subsequent base excis
70 ion of 5fC and 5caC by the DNA repair enzyme thymine DNA glycosylase (TDG), followed by base excision
71 aC are selectively recognized and excised by thymine DNA glycosylase (TDG), leading to DNA demethylat
72 e bases are recognized by the monofunctional thymine DNA glycosylase (Tdg), which cleaves the glycosi
74 e 5-halouracils in the context of the enzyme thymine DNA glycosylase (TDG), which is an enzyme that p
76 ollowed by replication-dependent dilution or thymine DNA glycosylase (TDG)-dependent base excision re
77 to cytosine through iterative oxidation and thymine DNA glycosylase (TDG)-mediated base excision rep
78 luorescent probe for real-time monitoring of thymine DNA glycosylase (TDG)-mediated BER of 5-formylcy
84 paired to regenerate unmodified cytosines by thymine-DNA glycosylase (TDG) and base excision repair (
91 ut has more recently been characterized as a thymine DNA glycosylase that interacts with the mismatch
92 e increased more than 20-fold, allowing each thymine DNA glycosylase to remove more than one uracil o
93 n of UNG1/2 but not by knockdown of SMUG1 or thymine-DNA glycosylase uracil-DNA glycosylases, proving
95 li genome as a sequence homolog of the human thymine DNA glycosylase with activity against mismatched