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1  than a conventional colorimetric assay with p-nitrophenyl phosphate.
2 nity and reacts faster with Cdc25B than does p-nitrophenyl phosphate.
3 ithout adversely affecting hydrolysis of bis-p-nitrophenyl phosphate.
4 mbda-Pase, which catalyzes hydrolysis of bis-p-nitrophenyl phosphate.
5 2) required for Ni2+-dependent hydrolysis of p-nitrophenyl phosphate.
6 toring of alkaline phosphatase hydrolysis of p-nitrophenyl phosphate.
7 ctivity on any other sugar phosphates, or on p-nitrophenyl phosphate.
8 coli alkaline phosphatases is 10-60% that of p-nitrophenyl phosphate.
9 ainst both purified phosphorylated Cps2D and p-nitrophenyl phosphate.
10 ase activity against the synthetic substrate p-nitrophenyl phosphate.
11 eavy-atom isotope effects with the substrate p-nitrophenyl phosphate.
12 ed with ATPase utilization of ATP but not of p-nitrophenyl phosphate.
13 ge of the RNA model compound 2-hydroxypropyl p-nitrophenyl phosphate.
14 ed for the cyclization/cleavage of 3'-uridyl p-nitrophenyl phosphate.
15  detectable activity with thymidine-3',5'-di(p-nitrophenyl)-phosphate.
16 d ATP, but was inhibited by MJ33 and diethyl p-nitrophenyl phosphate, a serine protease inhibitor.
17 upon the release of p-nitrophenol (pNP) from p-nitrophenyl phosphate, acid phosphatase activity was d
18 nd does not hydrolyze ATP, pyrophosphate, or p-nitrophenyl phosphate, although it hydrolyzes guanosin
19 ssays revealed catalytic activity toward bis-p-nitrophenyl phosphate, an indicator substrate for phos
20         Pretreatment of cp70 cells with bis-(p-nitrophenyl) phosphate, an esterase inhibitor, before
21 eriments using the small molecule substrates p-nitrophenyl phosphate and 3-O-methylfluorescein phosph
22 he catalytic properties were determined with p-nitrophenyl phosphate and compared to those of the nat
23 phosphorothioate, and the triesters, diethyl p-nitrophenyl phosphate and diethyl p-nitrophenyl phosph
24 ters measured herein for the diesters, ethyl p-nitrophenyl phosphate and ethyl p-nitrophenyl phosphor
25  the hydrolysis reactions of the monoesters, p-nitrophenyl phosphate and p-nitrophenyl phosphorothioa
26 ysis of the wild type and mutant PTP1B using p-nitrophenyl phosphate and phosphotyrosine-containing p
27 of (18)k(nuc) for hydrolysis of thymidine 5'-p-nitrophenyl phosphate and RNA cleavage by the RNase P
28 s, both enzymes were able to dephosphorylate p-nitrophenyl-phosphate and phosphotyrosine-containing s
29 ic phosphatase activity against nonspecific (p-nitrophenyl phosphate) and specific (CTD-PO(4)) substr
30 bda, the recombinant cores could use casein, p-nitrophenyl phosphate, and a wide variety of peptides
31 line phosphatase catalyzes the hydrolysis of p-nitrophenyl phosphate approximately 70 times faster th
32 Michaelis kinetic parameters, measured using p-nitrophenyl phosphate as a substrate, indicated that a
33 e Mn(2+)-dependent phosphatase activity with p-nitrophenyl phosphate as a substrate, showing that thi
34  full-length enzyme (kcat = 0.017 s-1), with p-nitrophenyl phosphate as substrate.
35 t is capable of utilizing phosphohistone and p-nitrophenyl phosphate as substrates.
36  phosphorylase a, RII peptide, Kemptide, and p-nitrophenyl phosphate as substrates.
37 assays with a low molecular weight substrate p-nitrophenyl phosphate as well as phosphocasein and apo
38 of the standard method based on colorimetric p-nitrophenyl phosphate assay.
39 antially altered catalytic activities toward p-nitrophenyl phosphate at pH 5.0, with both mutants exh
40 found that their in vitro sensitivity to bis-p-nitrophenyl phosphate (BNPP), however, was not shared
41 s the cleavage of the DNA model compound bis(p-nitrophenyl) phosphate (BNPP) in 80% DMSO solution at
42 atalytic activity toward the small substrate p-nitrophenyl phosphate, but is completely inactive towa
43 nt acceleration of the rate of hydrolysis of p-nitrophenyl phosphate by added dipolar solvents such a
44 o measured for the reaction of the monoester p-nitrophenyl phosphate by Ce(IV) bis-Tris propane (1.00
45  The assay is based on the hydrolysis of the p-nitrophenyl phosphate by intracellular acid phosphatas
46 ed by the serine protease inhibitor, diethyl p-nitrophenyl phosphate, by the tetrahedral mimic 1-hexa
47 bitors agree well with values determined for p-nitrophenyl phosphate cleavage.
48 tein was shown to catalyze the hydrolysis of p-nitrophenyl phosphate, dephosphorylate phosphotyrosyl,
49 hospholipids and phosphatase activity toward p-nitrophenyl phosphate, exhibits a visible absorption b
50 ly catalyzes the cleavage of 2-hydroxypropyl p-nitrophenyl phosphate (HPNP) and a number of diribonuc
51                 This preferred mechanism for p-nitrophenyl phosphate hydrolysis is difficult to find
52  3 orders of magnitude greater than that for p-nitrophenyl phosphate hydrolysis.
53 -rate profiles for the hydrolysis of diethyl p-nitrophenyl phosphate (I) and diethyl p-chlorophenyl p
54 te, 1.0 x 10(-2) M MgCl2, and 2.0 x 10(-4) M p-nitrophenyl phosphate in 1.0 M, pH 9.0 Tris buffer as
55 y is sensitive to the serine reagent diethyl p-nitrophenyl phosphate, indicating that RcOBL1 is a ser
56 example, the kcat/Km for SP-(-)-ethyl phenyl p-nitrophenyl phosphate is 1.8 x 10(8) M-1 s-1 but is on
57 tyrosine phosphatase catalyzed hydrolysis of p-nitrophenyl phosphate is characterized with the system
58  k(cat), as well as a large reduction in the p-nitrophenyl phosphate K(m) were observed for certain c
59 ar kinetics toward the artificial substrates p-nitrophenyl phosphate (k(cat)/K(m) = 15-25 M(-1) s(-1)
60 fission than the reaction of the more labile p-nitrophenyl phosphate (leaving group pK(a) = 7.14).
61 ative theoretical study of the hydrolysis of p-nitrophenyl phosphate, methyl phosphate and p-nitrophe
62 ving group were obtained for the reaction of p-nitrophenyl phosphate monoester coordinated to a dinuc
63                     The metal complex of the p-nitrophenyl phosphate monoester was found to hydrolyze
64   By contrast, the hydrolysis of uncomplexed p-nitrophenyl phosphate occurs by a very loose transitio
65  166 is replaced with an alanine, hydrolyzes p-nitrophenyl phosphate only about 3 times faster than p
66 rogated the phosphatase activity with either p-nitrophenyl phosphate or CTD-PO(4) as substrates.
67 inhibit recombinant human PTP1B using either p-nitrophenyl phosphate or the tyrosine-phosphorylated i
68                  The enthalpy of transfer of p-nitrophenyl phosphate (pNPP) and p-nitrophenyl phospho
69 ygen atoms in the AP-catalyzed hydrolysis of p-nitrophenyl phosphate (pNPP) and p-nitrophenylsulfate
70                In stopped-flow studies using p-nitrophenyl phosphate (pNPP) as a substrate, a burst o
71                                        Using p-nitrophenyl phosphate (pNPP) as a substrate, p34 is op
72 ement seen in parallel FCS experiments using p-nitrophenyl phosphate (pNPP) as substrate.
73 terase activity at 65 degrees C with ATP and p-nitrophenyl phosphate (pNPP) as substrates.
74 active mutant substrate complex of LTP1 with p-nitrophenyl phosphate (pNPP) at a resolution of 1.7 A.
75                            The hydrolysis of p-nitrophenyl phosphate (pNPP) catalyzed by calcineurin
76               The kcat for the hydrolysis of p-nitrophenyl phosphate (pNPP) decreases by factors of 6
77  pNPS anion are very similar to those of the p-nitrophenyl phosphate (pNPP) dianion.
78 fied that reversibly inhibited CD45-mediated p-nitrophenyl phosphate (pNPP) hydrolysis.
79  will hydrolyze small acylphosphates such as p-nitrophenyl phosphate (pNPP) in addition to ATP and ca
80                  ALP-catalyzed hydrolysis of p-nitrophenyl phosphate (pNPP) leads to the formation of
81  PP2A showed identical kinetics using either p-nitrophenyl phosphate (pNPP) or 32P-myelin basic prote
82                                              p-Nitrophenyl phosphate (PNPP) substrate, added to intac
83                             The reactions of p-nitrophenyl phosphate (pNPP) with the low-molecular ma
84 ave relied on the highly activated substrate p-nitrophenyl phosphate (pNPP), an aryl phosphate with a
85 heavy atom isotope analogue of the substrate p-nitrophenyl phosphate (pNPP).
86 the human dual-specific phosphatase VHR with p-nitrophenyl phosphate (pNPP).
87   The calculated kinetic isotope effects for p-nitrophenyl phosphate provide a means to discriminate
88 atio of activity versus IRS-1 to that versus p-nitrophenyl phosphate, PTP1B remained significantly mo
89 The enzyme catalyzes the rapid hydrolysis of p-nitrophenyl phosphate, ribose-5-phosphate, and phospho
90 ered with ATPase utilization of both ATP and p-nitrophenyl phosphate substrates, whereas derivatizati
91  ability to hydrolyze the phosphate group in p-nitrophenyl phosphate suggesting it had a critical rol
92 dition to the general phosphatase substrate, p-nitrophenyl phosphate, the heterodimeric form of the e
93 , binding limits k(cat)/K(m) for reaction of p-nitrophenyl phosphate, the most commonly employed subs
94                       For the diester, ethyl p-nitrophenyl phosphate, the nonbridge 18O effect for th
95     We report that CthPnkp also converts bis-p-nitrophenyl phosphate to p-nitrophenol and inorganic p
96 o HePTP on the HePTP-catalyzed hydrolysis of p-nitrophenyl phosphate, Tyr(P) peptides, and its physio
97 yl, ethyl, phenethyl, propargyl, phenyl, and p-nitrophenyl phosphate using [(16)O(18)O] labeled speci
98  as well as weak phosphatase activity toward p-nitrophenyl phosphate (V(max) = 0.08 micro mol/min. mg
99 60A for the S(P)-enantiomer of methyl phenyl p-nitrophenyl phosphate was 13000-fold greater than that
100 sly, the metal complex of the diester methyl-p-nitrophenyl phosphate was found to hydrolyze via a two
101 l chromophoric substrate, thymidine-3',5'-di(p-nitrophenyl)-phosphate, were studied.
102 nhibitor of the PTP1-catalyzed hydrolysis of p-nitrophenyl phosphate with a Ki of 4.9 +/- 0.7 microM.
103 rmined, and the best substrate found was bis(p-nitrophenyl) phosphate with a kcat/Km value of 6.7 x 1
104 ally efficient substrate identified was bis-(p-nitrophenyl) phosphate with a Km of 0.9 mM and a kcat

 
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