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3 structured RNA substrates reveals processive phosphorolytic activities for human Rrp41/Rrp45 and the
4 and adjacent normal tissues were assayed for phosphorolytic activity and sensitivity to 5-benzylacycl
7 No effect of nucleoside diphosphates on the phosphorolytic activity of E. coli PNPase was observed.
9 s, OIP2, is a 3'-->5' exoribonuclease with a phosphorolytic activity that processes the 3' terminus o
10 ns similar to the normal enzyme, and the new phosphorolytic activity was independent from thymidine p
11 llopentaose were the best substrates for the phosphorolytic and reverse synthetic reactions, respecti
12 ly determined values for G(ATP)P-T (ATP from phosphorolytic beta-glucan cleavage minus ATP for substr
13 bolically stable since they are resistant to phosphorolytic cleavage by pyrimidine nucleoside phospho
14 accharide uptake combined with intracellular phosphorolytic cleavage of beta-glucosidic bonds; and (i
15 gment that accumulates in the absence of the phosphorolytic enzymes revealed the presence of an exten
18 tide of the primer does not confer increased phosphorolytic excision by AZT(R) RT for all 3'-azido-dd
19 tural determinant important for the enhanced phosphorolytic excision of AZTMP associated with HIV res
20 primer terminus in the appropriate site for phosphorolytic excision of AZTMP by AZT-resistant (AZT(R
21 to 3'-azido-3'-deoxythymidine (AZT) involves phosphorolytic excision of chain-terminating AZT-5'-mono
22 nvolves reverse transcriptase (RT)-catalyzed phosphorolytic excision of the chain-terminating AZT-5'-
23 hypothesis, we evaluated the incorporation, phosphorolytic excision, and antiviral activity of a pan
25 d recombinant AtRrp41p displays a processive phosphorolytic exonuclease activity and requires a singl
26 ucleotide phosphorylase (PNPase), a 3'-to-5' phosphorolytic exoribonuclease, is thought to be the pri
29 ese results suggest that the requirement for phosphorolytic RNases for robust cellular growth and eff
31 he absence of the two known Escherichia coli phosphorolytic RNases, polynucleotide phosphorylase and
34 can unblock a chain-terminated DNA primer by phosphorolytic transfer of the terminal residue to an ac
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