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1 o covalent modification (adenylylation by GS adenylyltransferase).
2 s a nicotinic acid mononucleotide-preferring adenylyltransferase.
3 es of Fic proteins with those of other known adenylyltransferases.
4 ors is carried out by MccB THIF-type NAD/FAD adenylyltransferases.
5 rase (NAMPT) and nicotinamide mononucleotide adenylyltransferase 1 (NMNAT-1) constitute a nuclear NAD
8 (GAD), by the enzyme nicotinamide nucleotide adenylyltransferase 1 (NMNAT1) of the NAD(+) salvage pat
9 verexpression of nicotinamide mononucleotide adenylyltransferase 1 (Nmnat1) or exogenous application
11 ding sequence of nicotinamide mononucleotide adenylyltransferase 1 (Nmnat1), which alone is sufficien
13 ed redistribution of nicotinamide nucleotide adenylyltransferase 1 from nuclei to axons in primary ne
14 NAD(+) synthase nicotinamide mononucleotide adenylyltransferase-1 (NMNAT1) in the developing murine
16 thesizing enzyme nicotinamide mononucleotide adenylyltransferase 2 (NMNAT2) is a critical survival fa
19 evels of NMNAT2 (nicotinamide mononucleotide adenylyltransferase 2), a recently identified survival f
20 clear isoform of nicotinamide mononucleotide adenylyltransferase, a rate-limiting enzyme in nicotinam
21 by LigB, thus confirming that the ligase and adenylyltransferase activities are intrinsic to the LigB
23 igase is thermophilic in vitro, with optimal adenylyltransferase activity at 90 degrees C and nick-jo
24 untingtin yeast interacting protein E), with adenylyltransferase activity but unknown physiological t
25 rate that the PfhB2 Fic domains also possess adenylyltransferase activity that targets the switch 1 t
26 verexpression of GS in glnE mutants (lacking adenylyltransferase activity) also causes poor growth.
27 the primer is absolutely required for VP55's adenylyltransferase activity, but not for stable VP55-RN
28 ereas LigC and LigD, which have ATP-specific adenylyltransferase activity, display weak nick joining
30 lylation (inactivation) by a bifunctional GS adenylyltransferase/adenylyl-removing enzyme (ATase).
31 ggesting that GlnK-UMP is required to signal adenylyltransferase/adenylyl-removing enzyme-mediated de
32 pyrophosphorylase (AGP; glucose-1-phosphate adenylyltransferase; ADP: alpha-D-glucose-1-phosphate ad
33 ucose pyrophosphorylase (glucose-1-phosphate adenylyltransferase; ADP:alpha-D-glucose-1-phosphate ade
34 (ybeN) coding for nicotinate mononucleotide adenylyltransferase, an NAD(P) biosynthetic enzyme, has
36 tA antitoxin (MNT-domain protein) acts as an adenylyltransferase and chemically modifies the HepT tox
39 ridylyltransferase/uridylyl-removing enzyme, adenylyltransferase, and the kinase/phosphatase nitrogen
45 enzyme nicotinic acid mononucleotide (NaMN) adenylyltransferase (AT), is essential for the synthesis
46 es of the PII receptors glutamine synthetase adenylyltransferase (ATase) and the kinase/phosphatase n
47 ntrol the activities of glutamine synthetase adenylyltransferase (ATase) but did not affect the abili
49 II (NRII) and the glutamine synthetase (GS) adenylyltransferase (ATase), and is subject to reversibl
50 ate in a reconstituted system containing GS, adenylyltransferase (ATase), the PII signal transduction
52 biosynthetic enzymes, including a ThiF-like adenylyltransferase/cyclase that generates a C-terminal
54 recombinant bifunctional phosphopantetheine adenylyltransferase/dephospho-CoA kinase was kinetically
56 k depends on contacts to both the N-terminal adenylyltransferase domain and its signature C-terminal
57 no acid polypeptide composed of a C-terminal adenylyltransferase domain fused to a distinctive 126 am
58 stinctive structure composed of a C-terminal adenylyltransferase domain linked to an N-terminal modul
60 a sudden (NH4)+ upshift, strains lacking GS adenylyltransferase drain their glutamate pool into glut
61 eine decarboxylase (EC ), phosphopantetheine adenylyltransferase (EC ), and dephospho-CoA kinase (EC
62 transferase; ADP:alpha-D-glucose-1-phosphate adenylyltransferase, EC 2.7.7.27) catalyzes a key regula
63 ransferase; ADP: alpha-D-glucose-1-phosphate adenylyltransferase, EC 2.7.7.27), a key starch biosynth
65 tabolite of WldS/nicotinamide mononucleotide adenylyltransferase enzymatic activity, is sufficient an
66 n by both NMNAT (nicotinamide mononucleotide adenylyltransferase) expression and loss of wallenda/DLK
69 s the RFK activity, while the N-terminal FMN-adenylyltransferase (FMNAT) exhibits the FMNAT activity.
70 he core dinucleotide-binding fold with other adenylyltransferases from bacteria to human despite a li
73 utagenic exploration of the PPi motif in any adenylyltransferase is that the residues of the motif pa
74 dentify inhibitors of Mtb phosphopantetheine adenylyltransferase (MtbPPAT), the enzyme that catalyses
76 nstream enzymes of NAD synthesis, nicotinate adenylyltransferase (NadD family) and NAD synthetase (Na
77 of NAD biogenesis, nicotinate mononucleotide adenylyltransferase (NadD) and NAD synthetase (NadE), ar
78 lase subunit, probable nicotinate-nucleotide adenylyltransferase, NADH-quinone oxidoreductase, holo-[
80 on is catalyzed by nicotinate mononucleotide adenylyltransferase (NMAT), which is essential for bacte
82 f nicotinamide/nicotinic acid mononucleotide adenylyltransferase (NMNAT) act as a powerful suppressor
83 of NAD synthase nicotinamide mononucleotide adenylyltransferase (NMNAT) against activity-induced neu
84 , constituted by nicotinamide mononucleotide adenylyltransferase (NMNAT) and nicotinamide phosphoribo
85 , (ii) a central nicotinamide mononucleotide adenylyltransferase (NMNAT) domain, and (iii) a C-termin
86 synthesis enzyme nicotinamide mononucleotide adenylyltransferase (NMNAT) have uncovered a novel neuro
88 inamide/nicotinate mononucleotide (NMN/ NaMN)adenylyltransferase (NMNAT) is an indispensable enzyme i
90 verexpression of nicotinamide mononucleotide adenylyltransferase (Nmnat), a component of the slow Wal
91 Importantly, nicotinamide mononucleotide adenylyltransferase (NMNAT), an evolutionarily conserved
92 d nicotinamide/nicotinic acid mononucleotide adenylyltransferase (Nmnat), and we examined its effects
96 synthesis enzyme nicotinamide mononucleotide adenylyltransferase (NMNAT1) is frequently deleted in hu
98 s is mediated by nicotinamide mononucleotide adenylyltransferases (NMNATs), but their role in Parkins
101 ferring enzymes such as glutamine synthetase adenylyltransferase or kanamycin nucleotidyltransferase,
102 pathways, including three distantly related adenylyltransferases (orthologs of the E. coli genes nad
107 method was applied to 4'-phosphopantetheine adenylyltransferase (PPAT) from Mycobacterium abscessus
115 , the S. aureus NaMNAT represents a distinct adenylyltransferase subfamily identifiable in part by co
116 termined that Delta97nsP4 possesses terminal adenylyltransferase (TATase) activity, as it specificall
117 tein has metal ion-dependent RNA 3'-terminal adenylyltransferase (TATase) activity, while other nucle
118 in putative sulfate permease and not sulfate adenylyltransferase transcripts, suggesting a role for f
119 nd compare its activity with other known Fic adenylyltransferases, VopS (Vibrio outer protein S) from
120 sed biosynthetic pathway, two genes encoding adenylyltransferases were overexpressed and the resultin