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1 ore potent and more specific inhibitors of S-adenosylmethionine decarboxylase.
2 the decarboxylation reaction catalyzed by S-adenosylmethionine decarboxylase.
3 enzyme alphabeta dimer than with wild-type S-adenosylmethionine decarboxylase.
7 ck by polyamines increased the activity of S-adenosylmethionine decarboxylase 1 (AMD1), leading to de
9 S proteasome caused substantial losses of S-adenosylmethionine decarboxylase activity despite accumu
11 ic genes encoding spermidine biosynthesis: S-adenosylmethionine decarboxylase (AdoMetDC) and spermidi
15 orspermine [DENSPM]) at 1 microM; however, S-adenosylmethionine decarboxylase (AdoMetDC) depletion wa
17 with DFMO in combination with SAM486A, an S-adenosylmethionine decarboxylase (AdoMetDC) inhibitor, h
28 e 5' leader of the mammalian mRNA encoding S-adenosylmethionine decarboxylase (AdoMetDC) serves as a
29 ing and decarboxylation reactions of human S-adenosylmethionine decarboxylase (AdoMetDC), a critical
31 Previously we showed that trypanosomatid S-adenosylmethionine decarboxylase (AdoMetDC), a key enzym
33 bitor of the polyamine biosynthetic enzyme S-adenosylmethionine decarboxylase (AdoMetDC), is presentl
36 fusions of polyamine biosynthetic enzymes S-adenosylmethionine decarboxylase (AdoMetDC, speD) and am
38 nd arginine decarboxylase (ADC), arginase, S-adenosylmethionine decarboxylase (AdoMetDC/speD), spermi
39 ort X-ray structures of Trypanosoma brucei S-adenosylmethionine decarboxylase alone and in functional
41 trescine amidohydrolase in archaea, and of S-adenosylmethionine decarboxylase and ornithine decarboxy
42 rmidine from putrescine by the key enzymes S-adenosylmethionine decarboxylase and spermidine synthase
43 imental frameshift frequencies measured in S-adenosylmethionine-decarboxylase and antizyme mutants, a
44 thetic enzymes ornithine decarboxylase and S-adenosylmethionine decarboxylase, and upregulates spermi
46 in COS-7 cells prevents the degradation of S-adenosylmethionine decarboxylase antigen; however, even
47 cause of a deletion in the gene coding for S-adenosylmethionine decarboxylase are very sensitive to e
49 mination accelerates normal degradation of S-adenosylmethionine decarboxylase, as the rate of degrada
51 ess that is accelerated by inactivation of S-adenosylmethionine decarboxylase by substrate-mediated t
53 deletion-insertion in the gene coding for S-adenosylmethionine decarboxylase (Deltaspe2) have an abs
54 hyltetrahydrofolate:Hcy methyltransferase, S-adenosylmethionine decarboxylase, DNA methyltransferase
56 We have determined the structure of the S-adenosylmethionine decarboxylase from potato, Solanum tu
57 rated by isolation of His-tagged AdoMetDC (S-adenosylmethionine decarboxylase) from COS-7 cells co-tr
61 activities of ornithine decarboxylase and S-adenosylmethionine decarboxylase in a similar fashion.
62 the constitutively high activity of plant S-adenosylmethionine decarboxylases in the absence of putr
63 in the optimal structural requirements for S-adenosylmethionine decarboxylase inhibition and potentia
64 provide a framework for interpretation of S-adenosylmethionine decarboxylase inhibition data and sug
65 bitor alpha-difluoromethylornithine or the S-adenosylmethionine decarboxylase inhibitor MDL-73811 low
66 zone (MGBG), a polyamine analog and potent S-adenosylmethionine decarboxylase inhibitor, decreases HI
67 reading frame (uORF) in the mRNA encoding S-adenosylmethionine decarboxylase is a cis-acting element
68 reading frame (uORF) in the mRNA encoding S-adenosylmethionine decarboxylase is a polyamine-responsi
74 anosomatid spermidine biosynthetic enzyme, S-adenosylmethionine decarboxylase, is regulated by hetero
75 The availability of the recombinant H243A S-adenosylmethionine decarboxylase proenzyme provides a us
76 deoxyadenosine (MDL73811), an inhibitor of S-adenosylmethionine decarboxylase, resulted in increased
78 thesis, ornithine decarboxylase (ODC), and S-adenosylmethionine decarboxylase (SAMdc), were measured
79 ase), speC (ornithine decarboxylase), spe D (adenosylmethionine decarboxylase), speE (spermidine synt
80 n was horizontally acquired as a bacterial S-adenosylmethionine decarboxylase-SpmSyn fusion protein b
81 n levels of ornithine decarboxylase and of S-adenosylmethionine decarboxylase, two essential enzymes
82 ect evidence of peptide synthesis from the S-adenosylmethionine decarboxylase uORF using an in vitro