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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 embrane domain and cytoplasmic domain of the amidating enzyme, peptidylglycine alpha-amidating monoox
19 PCs), carboxypeptidase E, and peptidyl alpha-amidating enzyme, to transform recombinant precursors in
23 y we analyzed the expression of the peptidyl amidating enzymes in histological abnormalities found in
26 e of the peptidyl-alpha-hydroxyglycine alpha-amidating lyase (PAL) domain of peptidylglycine alpha-am
28 enzyme, peptidyl-alpha-hydroxyglycine alpha-amidating lyase (PAL, EC 4.3.2.5), has no known homologu
29 PHM, and peptidyl-alpha-hydroxyglycine alpha-amidating lyase or PAL) that in most eukaryotes are expr
30 The amidating enzyme, peptidyglycine alpha-amidating mono-oxygenase (PAM), the prohormone convertas
34 al domains of membrane peptidylglycine alpha-amidating monooxygenase (PAM) are essential for peptide
39 tide processing enzyme peptidylglycine alpha-amidating monooxygenase (PAM) contains signals that dire
40 g of integral membrane peptidylglycine alpha-amidating monooxygenase (PAM) in the neuroendocrine AtT-
41 n of membrane forms of peptidylglycine alpha-amidating monooxygenase (PAM) in the secretory pathway o
45 ing P-type ATPase, and peptidylglycine alpha-amidating monooxygenase (PAM), a copper-dependent membra
46 amined the turnover of peptidylglycine alpha-amidating monooxygenase (PAM), a membrane enzyme involve
47 for full activation by peptidylglycine alpha-amidating monooxygenase (PAM), a transmembrane vesicular
48 o catalytic domains of peptidylglycine alpha-amidating monooxygenase (PAM), a type I integral membran
49 ical tools to identify peptidylglycine alpha-amidating monooxygenase (PAM), a type I secretory granul
52 We recently identified peptidylglycine alpha-amidating monooxygenase (PAM), an enzyme required for ge
53 sis and trafficking of peptidylglycine alpha-amidating monooxygenase (PAM), an essential cuproenzyme
56 zing esterase/lipase, peptidyl glycine alpha-amidating monooxygenase (PAM), peptidase cleavage, and g
57 ion, we find that both peptidylglycine alpha-amidating monooxygenase (PAM), the enzyme responsible fo
65 egral membrane protein peptidylglycine alpha-amidating monooxygenase (PAM; EC 1.14.17.3) contains mul
66 he bifunctional enzyme peptidylglycine-alpha-amidating monooxygenase mediates the conversion of C-ter
68 glycine (hippurate) by peptidylglycine alpha-amidating monooxygenase to again yield benzamide and gly
69 lyase (PAL) domain of peptidylglycine alpha-amidating monooxygenase was investigated with respect to
70 processing enzyme PAM (peptidylglycine alpha-amidating monooxygenase) as tools to study the peptiderg
71 y its interaction with peptidylglycine alpha-amidating monooxygenase, an enzyme essential for neurope
72 or to the mature form, peptidylglycine alpha-amidating monooxygenase, were upregulated by inositol de
76 Removing the C-terminal alanine alone, or amidating the C terminus carboxyl group, also eliminated
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