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1 more potent and more specific inhibitors of S-adenosylmethionine decarboxylase.
2 of the decarboxylation reaction catalyzed by S-adenosylmethionine decarboxylase.
3 f enzyme alphabeta dimer than with wild-type S-adenosylmethionine decarboxylase.
4 ng stems from mTORC1-dependent regulation of S-adenosylmethionine decarboxylase 1 (AMD1) stability.
6 26 S proteasome caused substantial losses of S-adenosylmethionine decarboxylase activity despite accu
8 otic genes encoding spermidine biosynthesis: S-adenosylmethionine decarboxylase (AdoMetDC) and spermi
12 lnorspermine [DENSPM]) at 1 microM; however, S-adenosylmethionine decarboxylase (AdoMetDC) depletion
14 nt with DFMO in combination with SAM486A, an S-adenosylmethionine decarboxylase (AdoMetDC) inhibitor,
25 the 5' leader of the mammalian mRNA encoding S-adenosylmethionine decarboxylase (AdoMetDC) serves as
26 ssing and decarboxylation reactions of human S-adenosylmethionine decarboxylase (AdoMetDC), a critica
28 Previously we showed that trypanosomatid S-adenosylmethionine decarboxylase (AdoMetDC), a key enz
30 hibitor of the polyamine biosynthetic enzyme S-adenosylmethionine decarboxylase (AdoMetDC), is presen
33 ne fusions of polyamine biosynthetic enzymes S-adenosylmethionine decarboxylase (AdoMetDC, speD) and
34 eport X-ray structures of Trypanosoma brucei S-adenosylmethionine decarboxylase alone and in function
35 putrescine amidohydrolase in archaea, and of S-adenosylmethionine decarboxylase and ornithine decarbo
36 permidine from putrescine by the key enzymes S-adenosylmethionine decarboxylase and spermidine syntha
37 erimental frameshift frequencies measured in S-adenosylmethionine-decarboxylase and antizyme mutants,
38 ynthetic enzymes ornithine decarboxylase and S-adenosylmethionine decarboxylase, and upregulates sper
40 n in COS-7 cells prevents the degradation of S-adenosylmethionine decarboxylase antigen; however, eve
41 because of a deletion in the gene coding for S-adenosylmethionine decarboxylase are very sensitive to
43 samination accelerates normal degradation of S-adenosylmethionine decarboxylase, as the rate of degra
45 ocess that is accelerated by inactivation of S-adenosylmethionine decarboxylase by substrate-mediated
47 a deletion-insertion in the gene coding for S-adenosylmethionine decarboxylase (Deltaspe2) have an a
48 ethyltetrahydrofolate:Hcy methyltransferase, S-adenosylmethionine decarboxylase, DNA methyltransferas
51 strated by isolation of His-tagged AdoMetDC (S-adenosylmethionine decarboxylase) from COS-7 cells co-
55 he activities of ornithine decarboxylase and S-adenosylmethionine decarboxylase in a similar fashion.
56 in the constitutively high activity of plant S-adenosylmethionine decarboxylases in the absence of pu
57 tain the optimal structural requirements for S-adenosylmethionine decarboxylase inhibition and potent
58 re provide a framework for interpretation of S-adenosylmethionine decarboxylase inhibition data and s
59 hibitor alpha-difluoromethylornithine or the S-adenosylmethionine decarboxylase inhibitor MDL-73811 l
60 razone (MGBG), a polyamine analog and potent S-adenosylmethionine decarboxylase inhibitor, decreases
61 en reading frame (uORF) in the mRNA encoding S-adenosylmethionine decarboxylase is a cis-acting eleme
62 en reading frame (uORF) in the mRNA encoding S-adenosylmethionine decarboxylase is a polyamine-respon
68 ypanosomatid spermidine biosynthetic enzyme, S-adenosylmethionine decarboxylase, is regulated by hete
69 The availability of the recombinant H243A S-adenosylmethionine decarboxylase proenzyme provides a
70 '-deoxyadenosine (MDL73811), an inhibitor of S-adenosylmethionine decarboxylase, resulted in increase
72 ynthesis, ornithine decarboxylase (ODC), and S-adenosylmethionine decarboxylase (SAMdc), were measure
73 ion levels of ornithine decarboxylase and of S-adenosylmethionine decarboxylase, two essential enzyme
74 irect evidence of peptide synthesis from the S-adenosylmethionine decarboxylase uORF using an in vitr
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