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1 due that provides a substrate for endogenous amidating activity in the mammary gland.
2  show that PHM is required for peptide alpha-amidating activity throughout the life of Drosophila.
3  for maintaining appropriate levels of alpha-amidating activity under changing conditions in vivo.
4 chanism where the M(III) complex engages the amidating agent via oxidative coupling to form a M(V)-im
5                                        Novel amidating agents containing a 1,4,2-dioxazole moiety all
6 dation of thioamides with robust dioxazolone amidating agents via C(sp(3) )-H bond activation to gene
7           Bifunctional peptidylglycine alpha-amidating enzyme (alpha-AE) catalyzes the O2-dependent c
8           Bifunctional peptidylglycine alpha-amidating enzyme (alpha-AE) catalyzes the two-step conve
9 rs in the bifunctional peptidylglycine alpha-amidating enzyme (alpha-AE) have been investigated by EP
10  beta-hydroxylase and peptidyl glycine alpha-amidating enzyme also co-aggregated with granule content
11       The bifunctional peptidylglycine alpha-amidating enzyme catalyzes the C-terminal amidation of g
12 ses and other modifying enzymes, such as the amidating enzyme complex (PAM), in converting inactive o
13 omain was demonstrated with the bifunctional amidating enzyme of Xenopus laevis.
14  diverse amidated neuropeptides and with the amidating enzyme peptidylglycine alpha-hydroxylating mon
15 ystem to create mosaics for the neuropeptide amidating enzyme PHM; amidation is a highly specific and
16 bstrate specificity of peptidylglycine alpha-amidating enzyme was determined and compared against a c
17                                          The amidating enzyme, peptidyglycine alpha-amidating mono-ox
18 lopmentally regulated release of the peptide amidating enzyme, peptidylglycine alpha-amidating monoox
19 embrane domain and cytoplasmic domain of the amidating enzyme, peptidylglycine alpha-amidating monoox
20 PCs), carboxypeptidase E, and peptidyl alpha-amidating enzyme, to transform recombinant precursors in
21 ns, Dph1 to Dph5, and an as-yet-unidentified amidating enzyme.
22 oteins, Dph1 to -5, and a still unidentified amidating enzyme.
23                                 The peptidyl amidating enzymes have previously been identified in cel
24 y we analyzed the expression of the peptidyl amidating enzymes in histological abnormalities found in
25           The intense expression of peptidyl amidating enzymes in type II cell hyperplasia and atypic
26  of cells strongly positive for the peptidyl amidating enzymes.
27 , early response modifiers, and neuropeptide-amidating enzymes.
28 e of the peptidyl-alpha-hydroxyglycine alpha-amidating lyase (PAL) domain of peptidylglycine alpha-am
29 d lyase (peptidyl-alpha-hydroxyglycine alpha-amidating lyase (PAL)) domains.
30  enzyme, peptidyl-alpha-hydroxyglycine alpha-amidating lyase (PAL, EC 4.3.2.5), has no known homologu
31 PHM, and peptidyl-alpha-hydroxyglycine alpha-amidating lyase or PAL) that in most eukaryotes are expr
32   The amidating enzyme, peptidyglycine alpha-amidating mono-oxygenase (PAM), the prohormone convertas
33 nal enzyme called PAM (peptidylglycine alpha-amidating mono-oxygenase).
34 arboxypeptidase H, and peptidylglycine alpha-amidating mono-oxygenase.
35 ed B -0.33, P<0.001), and peptidyl-glycine a-amidating monooxygenase (AMD, fully adjusted B -0.32, P<
36                        Peptidylglycine alpha-amidating monooxygenase (PAM) (EC 1.14.17.3) catalyzes p
37 al domains of membrane peptidylglycine alpha-amidating monooxygenase (PAM) are essential for peptide
38                        Peptidylglycine alpha-amidating monooxygenase (PAM) catalyzes a two-step react
39                        Peptidylglycine alpha-amidating monooxygenase (PAM) catalyzes the amidation of
40                        Peptidylglycine alpha-amidating monooxygenase (PAM) catalyzes the carboxyl-ter
41                        Peptidylglycine alpha-amidating monooxygenase (PAM) catalyzes the COOH-termina
42 tide processing enzyme peptidylglycine alpha-amidating monooxygenase (PAM) contains signals that dire
43 g of integral membrane peptidylglycine alpha-amidating monooxygenase (PAM) in the neuroendocrine AtT-
44 n of membrane forms of peptidylglycine alpha-amidating monooxygenase (PAM) in the secretory pathway o
45                        Peptidylglycine alpha-amidating monooxygenase (PAM) is an enzyme expressed by
46                        Peptidylglycine alpha-amidating monooxygenase (PAM) is an essential enzyme tha
47                Because peptidylglycine alpha-amidating monooxygenase (PAM) is one of the few membrane
48                        Peptidylglycine alpha-amidating monooxygenase (PAM), a bifunctional enzyme, ca
49 ing P-type ATPase, and peptidylglycine alpha-amidating monooxygenase (PAM), a copper-dependent membra
50 amined the turnover of peptidylglycine alpha-amidating monooxygenase (PAM), a membrane enzyme involve
51 for full activation by peptidylglycine alpha-amidating monooxygenase (PAM), a transmembrane vesicular
52 o catalytic domains of peptidylglycine alpha-amidating monooxygenase (PAM), a type I integral membran
53 ical tools to identify peptidylglycine alpha-amidating monooxygenase (PAM), a type I secretory granul
54  in atrial granules is peptidylglycine alpha-amidating monooxygenase (PAM), an enzyme essential for a
55                        Peptidylglycine alpha-amidating monooxygenase (PAM), an enzyme essential for b
56                        Peptidylglycine alpha-amidating monooxygenase (PAM), an enzyme essential for n
57 We recently identified peptidylglycine alpha-amidating monooxygenase (PAM), an enzyme required for ge
58 sis and trafficking of peptidylglycine alpha-amidating monooxygenase (PAM), an essential cuproenzyme
59                        Peptidylglycine alpha-amidating monooxygenase (PAM), an integral membrane prot
60                        Peptidylglycine alpha-amidating monooxygenase (PAM), an integral membrane prot
61 uires a single enzyme, peptidylglycine alpha-amidating monooxygenase (PAM), and lack of amidation ren
62 tide amidating enzyme, peptidylglycine alpha-amidating monooxygenase (PAM), and the presence of pepti
63 zing esterase/lipase, peptidyl glycine alpha-amidating monooxygenase (PAM), peptidase cleavage, and g
64 ion, we find that both peptidylglycine alpha-amidating monooxygenase (PAM), the enzyme responsible fo
65 cyl-CoA synthetase and peptidylglycine alpha-amidating monooxygenase (PAM).
66  the amidating enzyme, peptidylglycine alpha-amidating monooxygenase (PAM).
67 es by the bifunctional enzyme peptidyl-alpha-amidating monooxygenase (PAM).
68 e bifunctional enzyme, peptidylglycine alpha-amidating monooxygenase (PAM).
69 he bifunctional enzyme peptidylglycine alpha-amidating monooxygenase (PAM).
70 outing determinants of peptidylglycine alpha-amidating monooxygenase (PAM).
71 essing is catalyzed by peptidylglycine alpha-amidating monooxygenase (PAM).
72 egral membrane protein peptidylglycine alpha-amidating monooxygenase (PAM; EC 1.14.17.3) contains mul
73 he bifunctional enzyme peptidylglycine-alpha-amidating monooxygenase mediates the conversion of C-ter
74 s of a single protein (peptidylglycine alpha-amidating monooxygenase or PAM).
75 glycine (hippurate) by peptidylglycine alpha-amidating monooxygenase to again yield benzamide and gly
76  lyase (PAL) domain of peptidylglycine alpha-amidating monooxygenase was investigated with respect to
77 processing enzyme PAM (peptidylglycine alpha-amidating monooxygenase) as tools to study the peptiderg
78 y its interaction with peptidylglycine alpha-amidating monooxygenase, an enzyme essential for neurope
79 or to the mature form, peptidylglycine alpha-amidating monooxygenase, were upregulated by inositol de
80 h its interaction with peptidylglycine-alpha-amidating monooxygenase.
81 89SP by treatment with peptidylglycine-alpha-amidating monooxygenase.
82 is(phenylsulfonyl)-imide) was explored as an amidating reagent for C8-amidation of quinoline N-oxide
83 oducts using user-friendly dioxazolone as an amidating reagent in the presence of a Rh(III)-catalyst.
84 of quinoline N-oxide using dioxazolone as an amidating reagent under mild conditions is disclosed.
85 xazolone, which is an environmentally benign amidating reagent.
86 I) catalysis in conjunction with dioxazolone amidating reagents and isopropanol as an environmentally
87    Removing the C-terminal alanine alone, or amidating the C terminus carboxyl group, also eliminated