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1 AANAT activity in these cells was rhythmic in both LD an
2 AANAT activity is high at night in darkness, low during
3 AANAT expression and melatonin secretion (1) increased i
4 AANAT is a globular protein consisting of an eight-stran
5 AANAT is also found in the retina, where melatonin is th
6 AANAT is bound in the central channel of the 14-3-3zeta
7 AANAT peptides containing either T31 or S205 associate w
8 AANAT Thr31 phosphorylation on its own can enhance catal
9 AANATs from Agnathans (lamprey) and Chondrichthyes (cats
10 for accurate K D measurements of 14-3-3zeta-AANAT interaction using 14-3-3zeta fluorescently labeled
11 ivity of arylalkylamine N-acetyltransferase (AANAT) and N-acetylserotonin O-methyl transferase (ASMT)
14 catalyzed by serotonin N-acetyltransferase (AANAT) in a reaction requiring acetyl coenzyme A (AcCoA)
16 sferase (arylalkylamine N-acetyltransferase (AANAT)) is a critical enzyme in the light-mediated regul
17 oxylase, arylalkylamine N-acetyltransferase (AANAT), and hydroxyindole-O-methyltransferase (HIOMT).
18 ivity of arylalkylamine N-acetyltransferase (AANAT), the penultimate enzyme in the melatonin pathway
19 gland by arylalkylamine N-acetyltransferase (AANAT), the penultimate enzyme in the synthesis of melat
20 tonin by arylalkylamine N-acetyltransferase (AANAT), which is predominantly expressed in the pineal g
23 sferase [arylalkylamine N-acetyltransferase (AANAT)] is a key circadian rhythm enzyme that drives the
26 ssion of arylalkylamine N-acetyltransferase (AANAT; the enzyme regulating melatonin synthesis) or inh
27 ssion of arylalkylamine N-acetyltransferase (AANAT; the rate-limiting enzyme for melatonin synthesis
28 sferase (arylalkylamine N-acetyltransferase, AANAT) in the pineal gland control the rhythmic producti
29 sferase (arylalkylamine N-acetyltransferase, AANAT) is a member of the GCN5 N-acetyltransferase (GNAT
30 sferase (arylalkylamine N-acetyltransferase, AANAT) mRNA in the chicken pineal gland exhibits a circa
31 ltransferase (serotonin N-acetyltransferase, AANAT, EC ) is the penultimate enzyme in melatonin synth
32 sferase (arylalkylamine N-acetyltransferase, AANAT, EC 2.3.1.87) is the first enzyme in the conversio
33 sferase (arylalkylamine N-acetyltransferase, AANAT, EC 2.3.1.87) is the penultimate enzyme in melaton
34 known as arylalkylamine N-acetyltransferase; AANAT) bound to a potent bisubstrate analog inhibitor ha
41 nd (2) effect of local modulation of biliary AANAT expression on the autocrine proliferative/secretor
43 lly synthesized and found to be processed by AANAT, although 20- and 60-fold less efficiently compare
53 into the active site of X-ray structures for AANAT, and in total 241 compounds were tested as inhibit
54 ptamine were also shown to be substrates for AANAT, again with reduced kcat and kcat/Km compared with
55 o have enzyme activity generally typical for AANAT family members, although the substrate preference
56 the most striking difference is that fungal AANATs lack the regulatory domains of the vertebrate enz
57 sting genetic markers, 8 known genes (GALR2, AANAT, ENVL, SFRS2, SEC14L, DNAH17, API4, and TK1), and
60 endence on the H122Q, H120Q, and H120Q/H122Q AANAT mutants, we show that His-122 (with an apparent pK
61 bed here, a cell line (1E7) expressing human AANAT (hAANAT) has been developed to study the human enz
62 lead to the design of analogs with improved AANAT inhibitory properties for in vivo applications.
66 ated in wild-type C3H/f(+/+) mice but not in AANAT-mutated C57BL/6J mice, in a circadian rhythm; TrkB
67 thesis of melatonin; a large daily rhythm in AANAT activity drives the daily rhythm in circulating me
68 re describe a regulatory/binding sequence in AANAT that encodes a cAMP-operated binding switch throug
69 l regulation involves phosphorylation on key AANAT Ser and Thr residues which results in 14-3-3zeta r
71 lso generated a doubly fluorescently labeled AANAT which can be used to assess the stability of this
72 hat binding of AANAT by 14-3-3zeta modulates AANAT's activity and affinity for its substrates by stab
73 cognized high-affinity 14-3-3-binding motifs AANAT protein binds to 14-3-3zeta through pT31 or pS205.
75 without markedly increasing the abundance of AANAT protein or the activity of AANAT in broken cell pr
76 bundance of AANAT protein or the activity of AANAT in broken cell preparations; and, that forskolin,
79 lographic analysis, indicate that binding of AANAT by 14-3-3zeta modulates AANAT's activity and affin
80 switch from dual to single pS205 binding of AANAT to 14-3-3 changes the Km for substrates by approxi
81 Phosphorylation of T31 promotes binding of AANAT to the dimeric 14-3-3 protein, which activates AAN
85 AANAT evolved from the nonvertebrate form of AANAT after the Cephalochordate-Vertebrate split over on
86 retinas from these groups express a form of AANAT that is compositionally, biochemically, and kineti
94 stulated to be important in the mechanism of AANAT based on prior x-ray structural and biochemical st
95 of light/dark and circadian oscillations of AANAT activity in cultured retinal cells prepared from 6
99 ffects of single and dual phosphorylation of AANAT on acetyltransferase activity and relative affinit
104 Development of light-dark regulation of AANAT activity appears to precede the circadian clock-co
105 e ability to express circadian regulation of AANAT activity is an intrinsic property of retinal cells
106 tend our understanding of cAMP regulation of AANAT activity, because it is currently thought that thi
108 for E6 cells displayed prominent rhythms of AANAT activity in both LD and DD, indicative of circadia
110 ding to 14-3-3 and the cellular stability of AANAT and are consistent with the view that Ser-205 phos
114 ding was also observed using humanized ovine AANAT, which has a different C-terminal sequence (Gly-Cy
115 to the three-dimensional structure of ovine AANAT catalytic core; however, an important structural e
124 e analysis revealed the presence of putative AANATs in other fungi but not in the nearly complete gen
126 A changes on a circadian basis, with retinal AANAT-1 mRNA peaking in late afternoon and pineal AANAT-
127 In the current study, a putative second AANAT cyclic AMP-dependent protein kinase phosphorylatio
128 x enhances melatonin production by shielding AANAT from dephosphorylation and/or proteolysis and by d
130 he middle of the subjective night suppressed AANAT activity, indicating that the enzyme activity in t
132 tyltransferase, AA-NAT, HGMW-approved symbol AANAT; EC 2.3.1.87) is the penultimate enzyme in melaton
144 ta demonstrate that the binding of 14-3-3 to AANAT is regulated by light, with dramatic functional co
150 ferase (arylalkylamine N-ace-tyltransferase (AANAT)) catalyzes the reaction of serotonin (or tryptami
156 nt with the hypotheses that the advent of VT-AANAT contributed to the evolution of the pineal gland a
157 volutionary rate estimation indicate that VT-AANAT evolved from the nonvertebrate form of AANAT after
158 n of the available genomes indicates that VT-AANAT is absent from other forms of life, including the
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