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1 ed to attack the glycosidic bond and promote phosphorolysis.
2 V-spectroscopic monitoring of 5-bromouridine phosphorolysis.
3 ous N-glycan core oligosaccharide by reverse phosphorolysis.
4 ffects of (p)ppGpp on the polymerization and phosphorolysis activities of PNPase from Streptomyces co
5 ioadenosine nucleosidase (MTAN) catalyze the phosphorolysis and hydrolysis of 5'-methylthioadenosine
6 proved to be susceptible to PNPHyor-mediated phosphorolysis, and a markedly decreased or increased cy
7       Rates of >50 s-1 were obtained for the phosphorolysis at 30 degrees C, so that when the phospho
8 tive site and reduces the energy barrier for phosphorolysis by 10 kcal.mol(-1).
9                  It is produced from inosine phosphorolysis by purine nucleoside phosphorylase (PNP).
10 nosine (F-dAdo) is a "subversive substrate." Phosphorolysis by TvPNP of F-dAdo, which is not a substr
11 y of the indicated substrates including: for phosphorolysis, higher chitin oliogsaccharides, (GlcNAc)
12 osphorylase (PNP) catalyzes N-ribosidic bond phosphorolysis in 6-oxypurine nucleosides and deoxynucle
13 se) catalyzes RNA polymerization and 3'-->5' phosphorolysis in vitro, but its roles in plant organell
14                 PNP catalyzes the reversible phosphorolysis of 2'-deoxypurine ribonucleosides to the
15                                Hydrolysis or phosphorolysis of 2AMTA forms 2,6-diaminopurine, a fluor
16 AP), a reported anticancer target, catalyzes phosphorolysis of 5'-methylthioadenosine to salvage S-ad
17                          The kinetics of the phosphorolysis of 7-methylated guanosine analogues catal
18                     ppGpp also inhibited the phosphorolysis of a model RNA substrate derived from the
19                                           By phosphorolysis of cellobiose, CbpA releases one activate
20 ith the high efficiency of PNPHyor-catalyzed phosphorolysis of cladribine to its less toxic base 2-ch
21 r reaction catalyzed by these enzymes is the phosphorolysis of GDP-D-glucose to GDP and D-glucose 1-p
22  Glycoside phosphorylases (GPs) catalyze the phosphorolysis of glycans into the corresponding sugar 1
23                                    Efficient phosphorolysis of natural 6-oxopurine and 6-aminopurine
24 o catalyze the polymerization of ADP and the phosphorolysis of poly(A).
25 phosphorylase (PNP) catalyzes the reversible phosphorolysis of purine (2'-deoxy)ribonucleosides to gi
26 ucleoside phosphorylase catalyzes reversible phosphorolysis of purine nucleosides and 2'-deoxypurine
27 ms a ribocation-like transition state in the phosphorolysis of purine nucleosides and fast protein mo
28 dopsis VTC2 and VTC5 enzymes catalyze simple phosphorolysis of the guanylylated enzyme, forming GDP a
29 icroM ADP, CDP, GDP, and UDP, the Km for the phosphorolysis of the substrate with the 3' stem-loop wa
30 Hyor cells and observed a rapid and complete phosphorolysis of this drug when it was exposed to the s
31           TP enzyme catalyzes the reversible phosphorolysis of thymidine to thymine and 2-deoxy-D-rib
32                         TP protein catalyzes phosphorolysis of thymidine to thymine and deoxyribose 1
33  phosphorylase (TP) catalyzes the reversible phosphorolysis of thymidine, maintaining nucleoside home
34 idine phosphorylase catalyzes the reversible phosphorolysis of uridine and 2'-deoxyuridine to generat
35         This enzyme catalyzes the reversible phosphorolysis of uridine to uracil and ribose 1-phospha
36 osphorylase (UPase) catalyzes the reversible phosphorolysis of uridine to uracil.
37 ty, and accelerate substrate turnover in the phosphorolysis reaction catalyzed by hPNP.
38         The potential energy surface for the phosphorolysis reaction for several snapshots taken from
39 nthesis direction and as the reactant in the phosphorolysis reaction; their interconversion can occur
40  due to their lack of an isosbestic point of phosphorolysis under moderately alkaline conditions.
41 omyces antibioticus, and Escherichia coli in phosphorolysis using substrates derived from the rpsO-pn
42 CB) and alpha-glucose 1-phosphate by reverse phosphorolysis, using enzymes cellodextrin phosphorylase
43                                 However, net phosphorolysis was not substantially increased, because