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1 ructures, and as a 5'-deoxyribose phosphate (dRP) lyase.
3 ng with a BER intermediate revealed that the dRP lyase active site resides in a 24-kDa domain of Pol
4 trometry and deletion analysis localized the dRP lyase active site to the C-terminal segment of Rev1'
7 her DNA polymerases and a repair factor with dRP lyase activity (pol lambda, pol iota, pol theta and
8 a possesses both DNA polymerase activity and dRP lyase activity and is sufficient to carry out base e
10 is cancer-associated variant has very little dRP lyase activity but retains its polymerase activity.
12 in their ability to support BER in vitro The dRP lyase activity in both of these proteins was confirm
13 tory effect of pyridoxal 5'-phosphate on the dRP lyase activity is consistent with involvement of a p
15 hese results imply that Pol beta-dependent 5'dRP lyase activity is the rate-limiting step in BER in t
16 nthesis by pol beta demonstrated that the 5'-dRP lyase activity lags behind the polymerase activity d
18 n of cytotoxic 5'dRP lesions, and that the 5'dRP lyase activity of Pol beta is required to restore re
20 as a nucleotidyl transferase but also has a dRP lyase activity that cleaves 5'-deoxyribose phosphate
22 Lys35 and Lys60 are significantly reduced in dRP lyase activity, consistent with the lower ssDNA bind
23 lanine mutant, K35A/K68A/K72A, was devoid of dRP lyase activity, suggesting that the effects of the a
24 dentify BER cofactors, especially those with dRP lyase activity, we used a Pol beta null cell extract
25 s important for DNA binding and contains the dRP lyase activity, which is the rate-limiting step in t
33 at human pol iota has deoxyribose phosphate (dRP) lyase activity and unusual specificity for activity
34 ncovered a weak 5'-deoxyribose phosphate (5'-dRP) lyase activity in mouse Rev1 and demonstrated the e
35 xcised by the 5'-deoxyribose-5-phosphate (5'-dRP) lyase activity of DNA polymerase beta (pol beta): h
36 a has intrinsic 5'-deoxyribose phosphate (5'-dRP) lyase activity that is involved in single-nucleotid
39 evaluate the BER capacity of the enzyme, the dRP lyase and DNA polymerase activities were characteriz
40 lease and DNA ligase I, pol iota can use its dRP lyase and polymerase activities to repair G*U and A*
41 We confirm that DNA pol gamma is an active dRP lyase and show that other members of the family A of
44 the pH profiles of beta-pol and 8-kDa domain dRP lyase catalytic efficiency exhibit a broad alkaline
45 system was found to be removal of dRP (i.e. dRP lyase), catalyzed by the amino-terminal domain of be
46 endonuclease, deoxyribonucleotide phosphate (dRP) lyase, DNA synthesis, and DNA ligase activities com
47 ormer indicates interactions of the 8 kDa 5'-dRP lyase domain of the second Pol beta molecule with th
49 at sensitivity of this activity suggests the dRP lyase function requires a three-dimensional protein
50 l beta catalyzes two key enzymatic steps: 5'-dRP lyase gap trimming and template-directed DNA synthes
51 unlike pol beta, may only be able to act as dRP lyases in repair of AP sites when they occur at low
52 fractory to the beta-elimination step of the dRP lyase mechanism, thus blocking single-nucleotide BER
53 s not in an optimal configuration for the 5'-dRP lyase reaction in the crystal structures of the clos
55 , representing a trapped intermediate in the dRP lyase reaction, was subjected to controlled proteoly
57 his limits the overall catalytic rate of the dRP lyase, so that family A DNA polymerases, unlike pol
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