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4 chanism where the M(III) complex engages the amidating agent via oxidative coupling to form a M(V)-im
6 dation of thioamides with robust dioxazolone amidating agents via C(sp(3) )-H bond activation to gene
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
12 ses and other modifying enzymes, such as the amidating enzyme complex (PAM), in converting inactive o
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
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
24 y we analyzed the expression of the peptidyl amidating enzymes in histological abnormalities found in
28 e of the peptidyl-alpha-hydroxyglycine alpha-amidating lyase (PAL) domain of peptidylglycine alpha-am
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
35 ed B -0.33, P<0.001), and peptidyl-glycine a-amidating monooxygenase (AMD, fully adjusted B -0.32, P<
37 al domains of membrane peptidylglycine alpha-amidating monooxygenase (PAM) are essential for peptide
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
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
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
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
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
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
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.
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