PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 31140554-0 2020 Polyamine synthesis enzyme AMD1 is closely associated with tumorigenesis and prognosis of human gastric cancers. Polyamines 0-9 adenosylmethionine decarboxylase 1 Homo sapiens 27-31 3429943-1 1986 The polyamine biosynthetic enzymes ODC and SAMDC show higher activity in carcinomatous human breast tissue than in uninvolved tissue of the same breast; the interconversion enzyme PAO shows significantly lower activity in carcinomatous than uninvolved tissue. Polyamines 4-13 adenosylmethionine decarboxylase 1 Homo sapiens 43-48 33203990-1 2021 Polyamines are critical elements in mammals, but it remains unknown whether adenosyl methionine decarboxylase (AMD1), a rate-limiting enzyme in polyamine synthesis, is required for myeloid leukemia. Polyamines 144-153 adenosylmethionine decarboxylase 1 Homo sapiens 111-115 33203990-5 2021 Mechanistically, AMD1 depletion induced loss of mitochondrial membrane potential and accumulation of reactive oxygen species (ROS), resulting in the differentiation of LSCs via oxidative stress and aberrant activation of unfolded protein response (UPR) pathway, which was partially rescued by the addition of polyamine. Polyamines 309-318 adenosylmethionine decarboxylase 1 Homo sapiens 17-21 2513802-1 1989 1-Amino-oxy-3-aminopropane (AOAP) was reported to inhibit several mammalian polyamine-biosynthetic enzymes in vitro, including ornithine decarboxylase (ODC) and S-adenosylmethionine decarboxylase (AdoMetDC) [Khomutov, Hyvonen, Karvonen, Kauppinen, Paalanen, Paulin, Eloranta, Pajula, Andersson & Poso (1985) Biochem. Polyamines 76-85 adenosylmethionine decarboxylase 1 Homo sapiens 161-195 2513802-1 1989 1-Amino-oxy-3-aminopropane (AOAP) was reported to inhibit several mammalian polyamine-biosynthetic enzymes in vitro, including ornithine decarboxylase (ODC) and S-adenosylmethionine decarboxylase (AdoMetDC) [Khomutov, Hyvonen, Karvonen, Kauppinen, Paalanen, Paulin, Eloranta, Pajula, Andersson & Poso (1985) Biochem. Polyamines 76-85 adenosylmethionine decarboxylase 1 Homo sapiens 197-205 2775206-1 1989 The rate-limiting enzymes in polyamine biosynthesis, ornithine decarboxylase (ODC) and S-adenosylmethionine decarboxylase (AdoMetDC), are negatively regulated by the polyamines spermidine and spermine. Polyamines 29-38 adenosylmethionine decarboxylase 1 Homo sapiens 87-121 2775206-1 1989 The rate-limiting enzymes in polyamine biosynthesis, ornithine decarboxylase (ODC) and S-adenosylmethionine decarboxylase (AdoMetDC), are negatively regulated by the polyamines spermidine and spermine. Polyamines 29-38 adenosylmethionine decarboxylase 1 Homo sapiens 123-131 2775206-1 1989 The rate-limiting enzymes in polyamine biosynthesis, ornithine decarboxylase (ODC) and S-adenosylmethionine decarboxylase (AdoMetDC), are negatively regulated by the polyamines spermidine and spermine. Polyamines 166-176 adenosylmethionine decarboxylase 1 Homo sapiens 87-121 2775206-1 1989 The rate-limiting enzymes in polyamine biosynthesis, ornithine decarboxylase (ODC) and S-adenosylmethionine decarboxylase (AdoMetDC), are negatively regulated by the polyamines spermidine and spermine. Polyamines 166-176 adenosylmethionine decarboxylase 1 Homo sapiens 123-131 2930498-3 1989 This increase in AdoMetDC activity was shown to be, at least partly, caused by enhanced synthesis of the enzyme, which most likely was induced by the change in cellular polyamine content. Polyamines 169-178 adenosylmethionine decarboxylase 1 Homo sapiens 17-25 31467246-0 2019 A polyamine-independent role for S-adenosylmethionine decarboxylase. Polyamines 2-11 adenosylmethionine decarboxylase 1 Homo sapiens 33-67 31467246-1 2019 The only known function of S-adenosylmethionine decarboxylase (AdoMetDC) is to supply, with its partner aminopropyltransferase enzymes such as spermidine synthase (SpdSyn), the aminopropyl donor for polyamine biosynthesis. Polyamines 199-208 adenosylmethionine decarboxylase 1 Homo sapiens 27-61 31467246-1 2019 The only known function of S-adenosylmethionine decarboxylase (AdoMetDC) is to supply, with its partner aminopropyltransferase enzymes such as spermidine synthase (SpdSyn), the aminopropyl donor for polyamine biosynthesis. Polyamines 199-208 adenosylmethionine decarboxylase 1 Homo sapiens 63-71 30323064-4 2018 The impact of polyamines on translation is highlighted by autoregulation of the translation of mRNAs encoding key metabolic and regulatory proteins in the polyamine biosynthesis pathway, including S-adenosylmethionine decarboxylase (AdoMetDC), antizyme (OAZ), and antizyme inhibitor 1 (AZIN1). Polyamines 14-24 adenosylmethionine decarboxylase 1 Homo sapiens 197-231 29906410-2 2018 Here, we describe an essential role for polyamine regulator AMD1 in driving cell migration at the wound edge. Polyamines 40-49 adenosylmethionine decarboxylase 1 Homo sapiens 60-64 29906410-8 2018 We demonstrate that keratinocytes respond to wounding by modulating polyamine regulator AMD1 in order to regulate downstream gene expression and promote cell migration. Polyamines 68-77 adenosylmethionine decarboxylase 1 Homo sapiens 88-92 30323064-4 2018 The impact of polyamines on translation is highlighted by autoregulation of the translation of mRNAs encoding key metabolic and regulatory proteins in the polyamine biosynthesis pathway, including S-adenosylmethionine decarboxylase (AdoMetDC), antizyme (OAZ), and antizyme inhibitor 1 (AZIN1). Polyamines 14-24 adenosylmethionine decarboxylase 1 Homo sapiens 233-241 30323064-4 2018 The impact of polyamines on translation is highlighted by autoregulation of the translation of mRNAs encoding key metabolic and regulatory proteins in the polyamine biosynthesis pathway, including S-adenosylmethionine decarboxylase (AdoMetDC), antizyme (OAZ), and antizyme inhibitor 1 (AZIN1). Polyamines 14-23 adenosylmethionine decarboxylase 1 Homo sapiens 197-231 30323064-4 2018 The impact of polyamines on translation is highlighted by autoregulation of the translation of mRNAs encoding key metabolic and regulatory proteins in the polyamine biosynthesis pathway, including S-adenosylmethionine decarboxylase (AdoMetDC), antizyme (OAZ), and antizyme inhibitor 1 (AZIN1). Polyamines 14-23 adenosylmethionine decarboxylase 1 Homo sapiens 233-241 29357564-0 2018 Re: mTORC1-Dependent AMD1 Regulation Sustains Polyamine Metabolism in Prostate Cancer. Polyamines 46-55 adenosylmethionine decarboxylase 1 Homo sapiens 21-25 30138353-6 2018 Simultaneously, curcumin down regulated spermidine/spermine N1-acetyltransferase (SSAT) activity and the biosynthetic enzymes ODC and S-adenosylmethionine decarboxylase (SAMDC), thereby diminishing intracellular polyamine pools. Polyamines 212-221 adenosylmethionine decarboxylase 1 Homo sapiens 170-175 29342137-0 2018 Corrigendum: mTORC1-dependent AMD1 regulation sustains polyamine metabolism in prostate cancer. Polyamines 55-64 adenosylmethionine decarboxylase 1 Homo sapiens 30-34 29644784-2 2018 We previously reported that the polyamine regulator AMD1 is critical for embryonic stem cell self-renewal. Polyamines 32-41 adenosylmethionine decarboxylase 1 Homo sapiens 52-56 28658205-0 2017 mTORC1-dependent AMD1 regulation sustains polyamine metabolism in prostate cancer. Polyamines 42-51 adenosylmethionine decarboxylase 1 Homo sapiens 17-21 29084986-5 2017 Our analysis corroborates the importance of previously known regulators of the pathway, such as Adenosylmethionine Decarboxylase 1 (AMD1) and uncovers novel enzymes predicted to be relevant for polyamine homeostasis. Polyamines 194-203 adenosylmethionine decarboxylase 1 Homo sapiens 96-130 29084986-5 2017 Our analysis corroborates the importance of previously known regulators of the pathway, such as Adenosylmethionine Decarboxylase 1 (AMD1) and uncovers novel enzymes predicted to be relevant for polyamine homeostasis. Polyamines 194-203 adenosylmethionine decarboxylase 1 Homo sapiens 132-136 26030749-2 2015 As a rate-limiting enzyme of the polyamine biosynthetic pathway, S-adenosylmethionine decarboxylase (AdoMetDC) has been an attractive drug target. Polyamines 33-42 adenosylmethionine decarboxylase 1 Homo sapiens 65-99 28642498-4 2017 Although the parasite may hijack the host"s biosynthesis pathway, it relies mainly upon its own arginase-AdoMetDC/ODC pathway to acquire the polyamines it needs to develop. Polyamines 141-151 adenosylmethionine decarboxylase 1 Homo sapiens 105-113 27102990-1 2016 Polyamine content, which is associated with tumor growth, can be regulated by ornithine decarboxylase (ODC) and S-adenosyl methionine decarboxylase (SAMDC), two key enzymes in polyamine biosynthesis. Polyamines 0-9 adenosylmethionine decarboxylase 1 Homo sapiens 112-147 27102990-1 2016 Polyamine content, which is associated with tumor growth, can be regulated by ornithine decarboxylase (ODC) and S-adenosyl methionine decarboxylase (SAMDC), two key enzymes in polyamine biosynthesis. Polyamines 0-9 adenosylmethionine decarboxylase 1 Homo sapiens 149-154 27102990-1 2016 Polyamine content, which is associated with tumor growth, can be regulated by ornithine decarboxylase (ODC) and S-adenosyl methionine decarboxylase (SAMDC), two key enzymes in polyamine biosynthesis. Polyamines 176-185 adenosylmethionine decarboxylase 1 Homo sapiens 112-147 27102990-1 2016 Polyamine content, which is associated with tumor growth, can be regulated by ornithine decarboxylase (ODC) and S-adenosyl methionine decarboxylase (SAMDC), two key enzymes in polyamine biosynthesis. Polyamines 176-185 adenosylmethionine decarboxylase 1 Homo sapiens 149-154 27102990-4 2016 When the nanoparticles were taken up by tumor cells via endocytosis and degraded in endosome, the released agmatine and SAMDC siRNA can synergistically inhibit polyamines biosynthesis, inducing inhibition of tumor proliferation. Polyamines 160-170 adenosylmethionine decarboxylase 1 Homo sapiens 120-125 25079701-1 2015 BACKGROUND: The study aimed to examine the association between genes encoding molecules in the ornithine decarboxylase (ODC)-polyamine pathway (ODC1, AMD1, NQO1, NOS2A, and OAZ2) and gastric cancer risk and whether the gene-phytoestrogen interaction modifies gastric cancer risk. Polyamines 125-134 adenosylmethionine decarboxylase 1 Homo sapiens 150-154 25079701-9 2015 CONCLUSIONS: Our findings suggest that common variants in the genes involved in the ODC pathway may contribute to the risk of gastric cancer possibly by modulating ODC polyamine biosynthesis or by interaction between isoflavones and NQO1, OAZ2, and AMD1. Polyamines 168-177 adenosylmethionine decarboxylase 1 Homo sapiens 249-253 26030749-2 2015 As a rate-limiting enzyme of the polyamine biosynthetic pathway, S-adenosylmethionine decarboxylase (AdoMetDC) has been an attractive drug target. Polyamines 33-42 adenosylmethionine decarboxylase 1 Homo sapiens 101-109 24112028-4 2014 The expression of PA biosynthesis (ADC, SAMDC, SPDS and SPMS) and catabolism (DAO and PAO) genes was systematically up-regulated by PAs. Polyamines 18-20 adenosylmethionine decarboxylase 1 Homo sapiens 40-45 23165208-2 2012 The polyamine pathway regulator AMD1 was recently implicated in ESC self-renewal and directed differentiation of ESCs to neural precursor cells (NPCs). Polyamines 4-13 adenosylmethionine decarboxylase 1 Homo sapiens 32-36 23260169-4 2013 Nevertheless, regulatory mechanisms explaining polyamine biosynthetic genes displaying dysregulated expression in suicide completers, including ornithine decarboxylase antizymes 1 and 2 (OAZ1 and OAZ2), S-adenosylmethionine decarboxylase (AMD1), and arginase 2 (ARG2), have yet to be elucidated. Polyamines 47-56 adenosylmethionine decarboxylase 1 Homo sapiens 239-243 23041351-7 2013 Moreover, transcriptional analysis of polyamine and proline metabolism genes (P5CS, P5CR, ADC, SPMS, SPDS, SAMDC, PAO, DAO) further supported the obtained data and revealed a complex SNP concentration-, time-, and developmental stage-dependent mechanism controlling endogenous proline and polyamine metabolite production. Polyamines 38-47 adenosylmethionine decarboxylase 1 Homo sapiens 107-112 23165208-7 2012 We propose that both Amd1 and Odc1 are essential regulators of ESCs and function to ensure high polyamine levels to promote ESC self-renewal. Polyamines 96-105 adenosylmethionine decarboxylase 1 Homo sapiens 21-25 21827754-3 2011 Here I show that diatom genomes possess signal peptide-containing gene fusions of bacterially-derived polyamine biosynthetic enzymes S-adenosylmethionine decarboxylase (AdoMetDC) and an aminopropyltransferase, sometimes fused to a eukaryotic histone N-methyltransferase domain, that potentially synthesize and N-methylate LCPA. Polyamines 102-111 adenosylmethionine decarboxylase 1 Homo sapiens 133-167 22722845-6 2012 Among the new tumour suppressors are adenosylmethionine decarboxylase 1 (AMD1) and eukaryotic translation initiation factor 5A (eIF5A), two genes associated with hypusine, a unique amino acid produced as a product of polyamine metabolism through a highly conserved pathway. Polyamines 217-226 adenosylmethionine decarboxylase 1 Homo sapiens 37-71 22722845-6 2012 Among the new tumour suppressors are adenosylmethionine decarboxylase 1 (AMD1) and eukaryotic translation initiation factor 5A (eIF5A), two genes associated with hypusine, a unique amino acid produced as a product of polyamine metabolism through a highly conserved pathway. Polyamines 217-226 adenosylmethionine decarboxylase 1 Homo sapiens 73-77 22008221-2 2012 We recently performed a global analysis of polyamine gene expression across the brains of suicide completers, and identified up-regulation of four genes, arginase II (ARG2), S-adenosylmethionine decarboxylase (AMD1), and antizymes 1 and 2 (OAZ1 and OAZ2), which play essential roles in polyamine biosynthesis. Polyamines 286-295 adenosylmethionine decarboxylase 1 Homo sapiens 210-214 22391449-2 2012 We describe a new role for Amd1 (adenosyl methionine decarboxylase), a key enzyme in the polyamine synthesis pathway, in regulating both ESC self-renewal and differentiation to the neural lineage. Polyamines 89-98 adenosylmethionine decarboxylase 1 Homo sapiens 27-31 22192816-3 2012 Instead trypanosomatid S-adenosylmethionine decarboxylase (AdoMetDC), which catalyzes a key step in the biosynthesis of the polyamine spermidine, is activated by dimerization with an inducible protein termed prozyme. Polyamines 124-133 adenosylmethionine decarboxylase 1 Homo sapiens 23-57 22192816-3 2012 Instead trypanosomatid S-adenosylmethionine decarboxylase (AdoMetDC), which catalyzes a key step in the biosynthesis of the polyamine spermidine, is activated by dimerization with an inducible protein termed prozyme. Polyamines 124-133 adenosylmethionine decarboxylase 1 Homo sapiens 59-67 21827754-3 2011 Here I show that diatom genomes possess signal peptide-containing gene fusions of bacterially-derived polyamine biosynthetic enzymes S-adenosylmethionine decarboxylase (AdoMetDC) and an aminopropyltransferase, sometimes fused to a eukaryotic histone N-methyltransferase domain, that potentially synthesize and N-methylate LCPA. Polyamines 102-111 adenosylmethionine decarboxylase 1 Homo sapiens 169-177 21827754-4 2011 Fusions of similar, alternatively configured domains but with a catalytically dead AdoMetDC and in one case a Tudor domain, may N-dimethylate and transfer multiple aminopropyl unit polyamines onto silaffin proteins. Polyamines 181-191 adenosylmethionine decarboxylase 1 Homo sapiens 83-91 20514439-1 2010 We have previously showed that platinum drugs up-regulate SSAT and SMO and down-regulate ODC and SAMDC in the polyamine pathway. Polyamines 110-119 adenosylmethionine decarboxylase 1 Homo sapiens 97-102 21413019-2 2011 The rate-limiting polyamine biosynthetic enzymes, ornithine decarboxylase (ODC) and S-adenosylmethionine decarboxylase, are essential for mammalian development, with knockout of the genes encoding these enzymes, Odc1 and Amd1, causing early embryonic lethality in mice. Polyamines 18-27 adenosylmethionine decarboxylase 1 Homo sapiens 221-225 21413019-5 2011 In muscle, androgens act via the androgen receptor to regulate expression of polyamine biosynthetic enzyme genes, including Odc1 and Amd1, which may be one mechanism via which androgens promote muscle growth. Polyamines 77-86 adenosylmethionine decarboxylase 1 Homo sapiens 133-137 23573001-2 2011 Therefore, the present work was carried out with the goal of generating transgenic tomato plants with human S-adenosylmethionine decarboxylase (samdc) gene, a key gene involved in biosynthesis of polyamines, viz. Polyamines 196-206 adenosylmethionine decarboxylase 1 Homo sapiens 108-142 23573001-2 2011 Therefore, the present work was carried out with the goal of generating transgenic tomato plants with human S-adenosylmethionine decarboxylase (samdc) gene, a key gene involved in biosynthesis of polyamines, viz. Polyamines 196-206 adenosylmethionine decarboxylase 1 Homo sapiens 144-149 17676832-2 2007 AdoMetDC is intimately involved in the biosynthesis of polyamines, which are essential for tumor progression and are elevated in numerous types of tumors. Polyamines 55-65 adenosylmethionine decarboxylase 1 Homo sapiens 0-8 19527050-1 2009 S-Adenosylmethionine decarboxylase (AdoMetDC) is a key enzyme in the polyamine biosynthetic pathway. Polyamines 69-78 adenosylmethionine decarboxylase 1 Homo sapiens 0-34 19527050-1 2009 S-Adenosylmethionine decarboxylase (AdoMetDC) is a key enzyme in the polyamine biosynthetic pathway. Polyamines 69-78 adenosylmethionine decarboxylase 1 Homo sapiens 36-44 19584241-0 2009 Inhibition of S-adenosylmethionine decarboxylase by inhibitor SAM486A connects polyamine metabolism with p53-Mdm2-Akt/protein kinase B regulation and apoptosis in neuroblastoma. Polyamines 79-88 adenosylmethionine decarboxylase 1 Homo sapiens 14-48 19584241-1 2009 S-adenosylmethionine decarboxylase (AdoMetDC) is an essential enzyme of polyamine (PA) biosynthesis, and both AdoMetDC and PA levels are often up-regulated in cancer cells. Polyamines 72-81 adenosylmethionine decarboxylase 1 Homo sapiens 0-34 19584241-1 2009 S-adenosylmethionine decarboxylase (AdoMetDC) is an essential enzyme of polyamine (PA) biosynthesis, and both AdoMetDC and PA levels are often up-regulated in cancer cells. Polyamines 72-81 adenosylmethionine decarboxylase 1 Homo sapiens 36-44 19584241-1 2009 S-adenosylmethionine decarboxylase (AdoMetDC) is an essential enzyme of polyamine (PA) biosynthesis, and both AdoMetDC and PA levels are often up-regulated in cancer cells. Polyamines 83-85 adenosylmethionine decarboxylase 1 Homo sapiens 0-34 19584241-1 2009 S-adenosylmethionine decarboxylase (AdoMetDC) is an essential enzyme of polyamine (PA) biosynthesis, and both AdoMetDC and PA levels are often up-regulated in cancer cells. Polyamines 83-85 adenosylmethionine decarboxylase 1 Homo sapiens 36-44 19584241-1 2009 S-adenosylmethionine decarboxylase (AdoMetDC) is an essential enzyme of polyamine (PA) biosynthesis, and both AdoMetDC and PA levels are often up-regulated in cancer cells. Polyamines 123-125 adenosylmethionine decarboxylase 1 Homo sapiens 0-34 18548481-0 2008 Effects of antisense RNA targeting of ODC and AdoMetDC on the synthesis of polyamine synthesis and cell growth in prostate cancer cells using a prostatic androgen-dependent promoter in adenovirus. Polyamines 75-84 adenosylmethionine decarboxylase 1 Homo sapiens 46-54 18548481-1 2008 PURPOSE: This study was designed to investigate the use of a prostatic androgen-dependent promoter to mediate antisense targeting of ornithine decarboxylase (ODC) and S-adenosylmethionine decarboxylase (AdoMetDC) and its effects on the synthesis of polyamine. Polyamines 249-258 adenosylmethionine decarboxylase 1 Homo sapiens 167-201 18548481-1 2008 PURPOSE: This study was designed to investigate the use of a prostatic androgen-dependent promoter to mediate antisense targeting of ornithine decarboxylase (ODC) and S-adenosylmethionine decarboxylase (AdoMetDC) and its effects on the synthesis of polyamine. Polyamines 249-258 adenosylmethionine decarboxylase 1 Homo sapiens 203-211 18548481-11 2008 CONCLUSIONS: The pADxsi-PSES-AdoMetDC-ODC-PolyA AV specifically inhibited the expression of ODC and AdoMetDC and the synthesis of polyamine, while it induced p21 expression, resulting in cell growth arrest in the G1 phase in prostate cancer cells but not in other cells. Polyamines 130-139 adenosylmethionine decarboxylase 1 Homo sapiens 29-37 18548481-11 2008 CONCLUSIONS: The pADxsi-PSES-AdoMetDC-ODC-PolyA AV specifically inhibited the expression of ODC and AdoMetDC and the synthesis of polyamine, while it induced p21 expression, resulting in cell growth arrest in the G1 phase in prostate cancer cells but not in other cells. Polyamines 130-139 adenosylmethionine decarboxylase 1 Homo sapiens 100-108 19787085-1 2008 S-adenosylmethionine decarboxylase (SAMDC) is an enzyme which converts S-adenosylmethione (SAM), a methyl donor, to decarboxylated SAM (dcSAM), an aminopropyl donor for polyamine biosynthesis. Polyamines 169-178 adenosylmethionine decarboxylase 1 Homo sapiens 0-34 19787085-1 2008 S-adenosylmethionine decarboxylase (SAMDC) is an enzyme which converts S-adenosylmethione (SAM), a methyl donor, to decarboxylated SAM (dcSAM), an aminopropyl donor for polyamine biosynthesis. Polyamines 169-178 adenosylmethionine decarboxylase 1 Homo sapiens 36-41 20124698-2 2010 S-Adenosylmethionine decarboxylase (AdoMetDC) is a critical pyruvoyl-dependent enzyme in the polyamine-biosynthetic pathway. Polyamines 93-102 adenosylmethionine decarboxylase 1 Homo sapiens 36-44 20095967-4 2009 The two key enzymes in the polyamine biosynthetic pathway, ODC (ornithine decarboxylase) and AdoMetDC (S-adenosylmethionine decarboxylase), are strongly regulated by feedback mechanisms at several levels, including transcriptional, translational and post-translational. Polyamines 27-36 adenosylmethionine decarboxylase 1 Homo sapiens 93-101 20095967-4 2009 The two key enzymes in the polyamine biosynthetic pathway, ODC (ornithine decarboxylase) and AdoMetDC (S-adenosylmethionine decarboxylase), are strongly regulated by feedback mechanisms at several levels, including transcriptional, translational and post-translational. Polyamines 27-36 adenosylmethionine decarboxylase 1 Homo sapiens 103-137 19584241-1 2009 S-adenosylmethionine decarboxylase (AdoMetDC) is an essential enzyme of polyamine (PA) biosynthesis, and both AdoMetDC and PA levels are often up-regulated in cancer cells. Polyamines 123-125 adenosylmethionine decarboxylase 1 Homo sapiens 36-44 19209891-1 2009 S-adenosylmethionine decarboxylase (AdoMetDC) is a critical enzyme in the polyamine biosynthetic pathway and depends on a pyruvoyl group for the decarboxylation process. Polyamines 74-83 adenosylmethionine decarboxylase 1 Homo sapiens 0-34 19209891-1 2009 S-adenosylmethionine decarboxylase (AdoMetDC) is a critical enzyme in the polyamine biosynthetic pathway and depends on a pyruvoyl group for the decarboxylation process. Polyamines 74-83 adenosylmethionine decarboxylase 1 Homo sapiens 36-44 19053272-1 2008 Putrescine (1,4-diaminobutane) activates the autoprocessing and decarboxylation reactions of human S-adenosylmethionine decarboxylase (AdoMetDC), a critical enzyme in the polyamine biosynthetic pathway. Polyamines 171-180 adenosylmethionine decarboxylase 1 Homo sapiens 99-133 19053272-1 2008 Putrescine (1,4-diaminobutane) activates the autoprocessing and decarboxylation reactions of human S-adenosylmethionine decarboxylase (AdoMetDC), a critical enzyme in the polyamine biosynthetic pathway. Polyamines 171-180 adenosylmethionine decarboxylase 1 Homo sapiens 135-143 17021820-6 2007 Mathematical/Statistical modeling of the data from time-course and concentration-effect experiments of gene expression from nine polyamine pathway genes represented on the HGU95Av2 chip, indicates that three biosynthetic pathway genes (SAMDC, ODC1 and SRM) are down-regulated and one catabolic pathway gene (SSAT) is up-regulated. Polyamines 129-138 adenosylmethionine decarboxylase 1 Homo sapiens 236-241 17558447-1 2007 Polyamine biosynthesis is controlled primarily by ornithine decarboxylase (ODC) and S-adenosylmethionine decarboxylase (AdoMetDC). Polyamines 0-9 adenosylmethionine decarboxylase 1 Homo sapiens 84-118 17558447-1 2007 Polyamine biosynthesis is controlled primarily by ornithine decarboxylase (ODC) and S-adenosylmethionine decarboxylase (AdoMetDC). Polyamines 0-9 adenosylmethionine decarboxylase 1 Homo sapiens 120-128 17558447-5 2007 Our study showed that adenovirus-mediated antisense ODC and AdoMetDC expression inhibits tumor cell growth through blocking the polyamine synthesis pathway. Polyamines 128-137 adenosylmethionine decarboxylase 1 Homo sapiens 60-68 16490173-1 2006 AIM: To construct a recombinant adenovirus that can simultaneously express both antisense ornithine decarboxylase (ODC) and adenosylmethionine decarboxylase ( AdoMetDC ) and detect its inhibitory effect on the intracellular polyamine pool and colorectal cancer cell growth. Polyamines 224-233 adenosylmethionine decarboxylase 1 Homo sapiens 124-156 17593800-1 2007 S-adenosylmethionine decarboxylase (SAMDC) is an essential enzyme for the synthesis of spermidine and spermine in the biosynthetic pathway of polyamines. Polyamines 142-152 adenosylmethionine decarboxylase 1 Homo sapiens 0-34 17593800-1 2007 S-adenosylmethionine decarboxylase (SAMDC) is an essential enzyme for the synthesis of spermidine and spermine in the biosynthetic pathway of polyamines. Polyamines 142-152 adenosylmethionine decarboxylase 1 Homo sapiens 36-41 16941339-1 2006 S-adenosylmethionine decarboxylase (SAMDC), a key enzyme in polyamine biosynthesis, can be specifically inhibited by the experimental drug SAM486A. Polyamines 60-69 adenosylmethionine decarboxylase 1 Homo sapiens 0-34 16941339-1 2006 S-adenosylmethionine decarboxylase (SAMDC), a key enzyme in polyamine biosynthesis, can be specifically inhibited by the experimental drug SAM486A. Polyamines 60-69 adenosylmethionine decarboxylase 1 Homo sapiens 36-41 16783835-0 2006 Polyamine depletion by ODC-AdoMetDC antisense adenovirus impairs human colorectal cancer growth and invasion in vitro and in vivo. Polyamines 0-9 adenosylmethionine decarboxylase 1 Homo sapiens 27-35 16783835-1 2006 BACKGROUND: Polyamine biosynthesis is controlled primarily by ornithine decarboxylase (ODC) and S-adenosylmethionine decarboxylase (AdoMetDC). Polyamines 12-21 adenosylmethionine decarboxylase 1 Homo sapiens 96-130 16783835-1 2006 BACKGROUND: Polyamine biosynthesis is controlled primarily by ornithine decarboxylase (ODC) and S-adenosylmethionine decarboxylase (AdoMetDC). Polyamines 12-21 adenosylmethionine decarboxylase 1 Homo sapiens 132-140 16783835-9 2006 RESULTS: Our study demonstrated that adenovirus-mediated ODC and AdoMetDC antisense expression inhibits tumor cell growth through a blockade of the polyamine synthesis pathway. Polyamines 148-157 adenosylmethionine decarboxylase 1 Homo sapiens 65-73 16490173-1 2006 AIM: To construct a recombinant adenovirus that can simultaneously express both antisense ornithine decarboxylase (ODC) and adenosylmethionine decarboxylase ( AdoMetDC ) and detect its inhibitory effect on the intracellular polyamine pool and colorectal cancer cell growth. Polyamines 224-233 adenosylmethionine decarboxylase 1 Homo sapiens 159-167 16490173-9 2006 Western blotting demonstrated that both ODC and AdoMetDC were downregulated by Ad-ODC-AdoMetDCas, and consequently 3 kinds of polyamine (putrescine, spermidine and spermine) were reduced to very low levels. Polyamines 126-135 adenosylmethionine decarboxylase 1 Homo sapiens 48-56 16515461-1 2006 S-adenosylmethionine decarboxylase (AdoMetDC) is a key enzyme in the biosynthesis of the polyamines spermidine and spermine. Polyamines 89-99 adenosylmethionine decarboxylase 1 Homo sapiens 0-34 16257247-1 2006 In the malaria parasite, the two main regulatory activities of polyamine biosynthesis, ornithine decarboxylase (ODC) and S-adenosylmethionine decarboxylase (AdoMetDC) occur in a single bifunctional protein. Polyamines 63-72 adenosylmethionine decarboxylase 1 Homo sapiens 121-155 16257247-1 2006 In the malaria parasite, the two main regulatory activities of polyamine biosynthesis, ornithine decarboxylase (ODC) and S-adenosylmethionine decarboxylase (AdoMetDC) occur in a single bifunctional protein. Polyamines 63-72 adenosylmethionine decarboxylase 1 Homo sapiens 157-165 16515461-1 2006 S-adenosylmethionine decarboxylase (AdoMetDC) is a key enzyme in the biosynthesis of the polyamines spermidine and spermine. Polyamines 89-99 adenosylmethionine decarboxylase 1 Homo sapiens 36-44 16007177-3 2005 Treatment with DFMO in combination with SAM486A, an S-adenosylmethionine decarboxylase (AdoMetDC) inhibitor, has been shown to enhance polyamine pool depletion. Polyamines 135-144 adenosylmethionine decarboxylase 1 Homo sapiens 52-86 16007177-3 2005 Treatment with DFMO in combination with SAM486A, an S-adenosylmethionine decarboxylase (AdoMetDC) inhibitor, has been shown to enhance polyamine pool depletion. Polyamines 135-144 adenosylmethionine decarboxylase 1 Homo sapiens 88-96 15521072-3 2005 In the current studies, we examined the role of one of these genes, the polyamine pathway biosynthetic enzyme S-adenosylmethionine decarboxylase (SAM-DC) and the related enzyme, ornithine decarboxylase (ODC), on HSG cell differentiation during culture on extracellular matrix. Polyamines 72-81 adenosylmethionine decarboxylase 1 Homo sapiens 110-144 15868382-9 2005 Serial biopsy in one patient showed alterations in polyamines consistent with SAMDC inhibition. Polyamines 51-61 adenosylmethionine decarboxylase 1 Homo sapiens 78-83 15521072-3 2005 In the current studies, we examined the role of one of these genes, the polyamine pathway biosynthetic enzyme S-adenosylmethionine decarboxylase (SAM-DC) and the related enzyme, ornithine decarboxylase (ODC), on HSG cell differentiation during culture on extracellular matrix. Polyamines 72-81 adenosylmethionine decarboxylase 1 Homo sapiens 146-152 12653652-3 2003 S-Adenosylmethionine decarboxylase (AdoMetDC) is a key enzyme in polyamine biosynthesis and both mammalian and plant AdoMetDCs are translationally regulated by uORFs in response to polyamine levels by distinct mechanisms. Polyamines 65-74 adenosylmethionine decarboxylase 1 Homo sapiens 0-34 15821146-1 2005 S-Adenosylmethionine decarboxylase (SAMDC; EC 4.1.1.50) is a key rate-limiting enzyme located in the polyamine biosynthesis pathway. Polyamines 101-110 adenosylmethionine decarboxylase 1 Homo sapiens 0-34 15821146-1 2005 S-Adenosylmethionine decarboxylase (SAMDC; EC 4.1.1.50) is a key rate-limiting enzyme located in the polyamine biosynthesis pathway. Polyamines 101-110 adenosylmethionine decarboxylase 1 Homo sapiens 36-41 16170669-6 2005 Treatment of cells with a second inhibitor of polyamine biosynthesis, the S-adenosylmethionine decarboxylase (SAMDC) inhibitor SAM486A, also resulted in a dosage dependent decrease in meprin alpha and MMP-7 mRNA. Polyamines 46-55 adenosylmethionine decarboxylase 1 Homo sapiens 74-108 16170669-6 2005 Treatment of cells with a second inhibitor of polyamine biosynthesis, the S-adenosylmethionine decarboxylase (SAMDC) inhibitor SAM486A, also resulted in a dosage dependent decrease in meprin alpha and MMP-7 mRNA. Polyamines 46-55 adenosylmethionine decarboxylase 1 Homo sapiens 110-115 15704548-1 2004 Ornithine decarboxylase (ODC) and S-adenosylmethionine decarboxylase (AdoMetDC) are two key enzymes in polyamine (PA) biosynthesis and their inhibition leads to PA pool depletion and cell growth arrest. Polyamines 103-112 adenosylmethionine decarboxylase 1 Homo sapiens 34-68 15704548-1 2004 Ornithine decarboxylase (ODC) and S-adenosylmethionine decarboxylase (AdoMetDC) are two key enzymes in polyamine (PA) biosynthesis and their inhibition leads to PA pool depletion and cell growth arrest. Polyamines 103-112 adenosylmethionine decarboxylase 1 Homo sapiens 70-78 15704548-1 2004 Ornithine decarboxylase (ODC) and S-adenosylmethionine decarboxylase (AdoMetDC) are two key enzymes in polyamine (PA) biosynthesis and their inhibition leads to PA pool depletion and cell growth arrest. Polyamines 114-116 adenosylmethionine decarboxylase 1 Homo sapiens 34-68 15704548-1 2004 Ornithine decarboxylase (ODC) and S-adenosylmethionine decarboxylase (AdoMetDC) are two key enzymes in polyamine (PA) biosynthesis and their inhibition leads to PA pool depletion and cell growth arrest. Polyamines 114-116 adenosylmethionine decarboxylase 1 Homo sapiens 70-78 15704548-1 2004 Ornithine decarboxylase (ODC) and S-adenosylmethionine decarboxylase (AdoMetDC) are two key enzymes in polyamine (PA) biosynthesis and their inhibition leads to PA pool depletion and cell growth arrest. Polyamines 161-163 adenosylmethionine decarboxylase 1 Homo sapiens 34-68 15704548-1 2004 Ornithine decarboxylase (ODC) and S-adenosylmethionine decarboxylase (AdoMetDC) are two key enzymes in polyamine (PA) biosynthesis and their inhibition leads to PA pool depletion and cell growth arrest. Polyamines 161-163 adenosylmethionine decarboxylase 1 Homo sapiens 70-78 14535654-5 2003 The high activities of ornithine decarboxylase (ODC) and S-adenosylmethionine decarboxylase (AdoMetDC) in rapidly growing tissues and cells, particularly in tumour cells, suggested PA biosynthesis as a target for antineoplastic therapy. Polyamines 181-183 adenosylmethionine decarboxylase 1 Homo sapiens 57-91 14535654-5 2003 The high activities of ornithine decarboxylase (ODC) and S-adenosylmethionine decarboxylase (AdoMetDC) in rapidly growing tissues and cells, particularly in tumour cells, suggested PA biosynthesis as a target for antineoplastic therapy. Polyamines 181-183 adenosylmethionine decarboxylase 1 Homo sapiens 93-101 12974388-1 2003 S-Adenosylmethionine decarboxylase (AdoMetDC) is a key enzyme in polyamine biosynthesis. Polyamines 65-74 adenosylmethionine decarboxylase 1 Homo sapiens 36-44 12974388-3 2003 The AdoMetDC of the filarial parasite Onchocerca volvulus, however, is not only stimulated by putrescine but also by the naturally occuring polyamines spermidine and spermine. Polyamines 140-150 adenosylmethionine decarboxylase 1 Homo sapiens 4-12 12974388-8 2003 Bis(aralkyl)- and bis(alkyl)-substituted polyamine analogues with a 3-7-3 backbone were found to inhibit AdoMetDC activities, however, probably without interfering with the putrescine stimulation. Polyamines 41-50 adenosylmethionine decarboxylase 1 Homo sapiens 105-113 12686127-6 2003 These residues, Cys360 in ornithine decarboxylase (ODC) and Cys82 in AdoMetDC, react readily with nitric oxide (NO), which is therefore a potent inactivator of polyamine synthesis. Polyamines 160-169 adenosylmethionine decarboxylase 1 Homo sapiens 69-77 12653652-3 2003 S-Adenosylmethionine decarboxylase (AdoMetDC) is a key enzyme in polyamine biosynthesis and both mammalian and plant AdoMetDCs are translationally regulated by uORFs in response to polyamine levels by distinct mechanisms. Polyamines 65-74 adenosylmethionine decarboxylase 1 Homo sapiens 36-44 12653652-3 2003 S-Adenosylmethionine decarboxylase (AdoMetDC) is a key enzyme in polyamine biosynthesis and both mammalian and plant AdoMetDCs are translationally regulated by uORFs in response to polyamine levels by distinct mechanisms. Polyamines 181-190 adenosylmethionine decarboxylase 1 Homo sapiens 0-34 12653652-3 2003 S-Adenosylmethionine decarboxylase (AdoMetDC) is a key enzyme in polyamine biosynthesis and both mammalian and plant AdoMetDCs are translationally regulated by uORFs in response to polyamine levels by distinct mechanisms. Polyamines 181-190 adenosylmethionine decarboxylase 1 Homo sapiens 36-44 12624736-5 2003 SW620 cells grow faster, and the key regulatory enzymes of polyamine biosynthesis (ODC and AdoMetDC) are more active in the metastatic cells. Polyamines 59-68 adenosylmethionine decarboxylase 1 Homo sapiens 91-99 12600205-1 2003 S-Adenosylmethionine decarboxylase (AdoMetDC) is a pyruvoyl-dependent enzyme that catalyzes the formation of the aminopropyl group donor in the biosynthesis of the polyamines spermidine and spermine. Polyamines 164-174 adenosylmethionine decarboxylase 1 Homo sapiens 0-34 12600205-1 2003 S-Adenosylmethionine decarboxylase (AdoMetDC) is a pyruvoyl-dependent enzyme that catalyzes the formation of the aminopropyl group donor in the biosynthesis of the polyamines spermidine and spermine. Polyamines 164-174 adenosylmethionine decarboxylase 1 Homo sapiens 36-44 12674502-1 2003 S-Adenosylmethionine decarboxylase (AdoMetDC) is a key enzyme of the polyamine synthetic pathway providing decarboxylated S-adenosylmethionine for the formation of spermidine and spermine, respectively. Polyamines 69-78 adenosylmethionine decarboxylase 1 Homo sapiens 36-44 12114416-1 2002 PURPOSE: SAM486A is a novel inhibitor of the polyamine biosynthetic enzyme S-adenosylmethionine decarboxylase (SAMDC). Polyamines 45-54 adenosylmethionine decarboxylase 1 Homo sapiens 75-109 12114416-1 2002 PURPOSE: SAM486A is a novel inhibitor of the polyamine biosynthetic enzyme S-adenosylmethionine decarboxylase (SAMDC). Polyamines 45-54 adenosylmethionine decarboxylase 1 Homo sapiens 111-116 12114416-14 2002 Pharmacodynamic assessment of tumoral tissues in 1 study patient demonstrated changes in the levels of polyamines and their biosynthetic enzymes consistent with SAMDC inhibition. Polyamines 103-113 adenosylmethionine decarboxylase 1 Homo sapiens 161-166 33874627-3 2001 The polyamine response to inoculation was analysed by measuring activity and gene expression of S-adenosylmethionine decarboxylase (SAMDC), arginine-(ADC) and ornithine decarboxylases (ODC); incorporation of labelled putrescine; and activity of diamine oxidase (DAO). Polyamines 4-13 adenosylmethionine decarboxylase 1 Homo sapiens 132-137 12083379-8 2002 The results of this study which established correlations between alterations in the expression of ODC and SAMDC, the key rate limiting and regulatory activities in the synthesis of cellular polyamines, and malignant potential as a consequence of K-FGF overexpression supports a model which suggests that growth factor modulation of ODC and SAMDC expression is part of the altered growth regulatory program associated with cellular transformation and malignant progression. Polyamines 190-200 adenosylmethionine decarboxylase 1 Homo sapiens 106-111 11787064-1 2002 Mammalian S-adenosylmethionine decarboxylase (SAMDC) is a regulatory activity, which is involved in the biosynthesis of polyamines. Polyamines 120-130 adenosylmethionine decarboxylase 1 Homo sapiens 10-44 11787064-1 2002 Mammalian S-adenosylmethionine decarboxylase (SAMDC) is a regulatory activity, which is involved in the biosynthesis of polyamines. Polyamines 120-130 adenosylmethionine decarboxylase 1 Homo sapiens 46-51 11390378-1 2001 In the human malaria parasite Plasmodium falciparum (Pf), polyamines are synthesized by a bifunctional enzyme that possesses both ornithine decarboxylase (ODC) and S-adenosyl-l-methionine decarboxylase (AdoMetDC) activities. Polyamines 58-68 adenosylmethionine decarboxylase 1 Homo sapiens 203-211 11390378-4 2001 The biological advantage of the plasmodial bifunctional ODC/AdoMetDC might be that the control of polyamine synthesis is achieved by only having to regulate the abundance and activity of one protein. Polyamines 98-107 adenosylmethionine decarboxylase 1 Homo sapiens 60-68 11333018-1 2001 In mammals, control of S-adenosylmethionine decarboxylase (AdoMetDC) translation is one component of a feedback network that regulates intracellular levels of the polyamines, spermidine, and spermine. Polyamines 163-173 adenosylmethionine decarboxylase 1 Homo sapiens 23-57 11333018-1 2001 In mammals, control of S-adenosylmethionine decarboxylase (AdoMetDC) translation is one component of a feedback network that regulates intracellular levels of the polyamines, spermidine, and spermine. Polyamines 163-173 adenosylmethionine decarboxylase 1 Homo sapiens 59-67 11333018-2 2001 AdoMetDC mRNA from mammals contains a highly conserved upstream open reading frame (uORF) within its leader sequence that confers polyamine-regulated suppression of translation on the associated downstream cistron. Polyamines 130-139 adenosylmethionine decarboxylase 1 Homo sapiens 0-8 11333018-6 2001 Nevertheless, the mammalian AdoMetDC uORF, when introduced into a polyamine auxotroph of yeast, conferred polyamine regulation of both translational efficiency and ribosome loading on the associated mRNA. Polyamines 66-75 adenosylmethionine decarboxylase 1 Homo sapiens 28-36 11333018-6 2001 Nevertheless, the mammalian AdoMetDC uORF, when introduced into a polyamine auxotroph of yeast, conferred polyamine regulation of both translational efficiency and ribosome loading on the associated mRNA. Polyamines 106-115 adenosylmethionine decarboxylase 1 Homo sapiens 28-36 11489903-0 2001 Polyamine regulation of ribosome pausing at the upstream open reading frame of S-adenosylmethionine decarboxylase. Polyamines 0-9 adenosylmethionine decarboxylase 1 Homo sapiens 79-113 11489903-1 2001 Synthesis of S-adenosylmethionine decarboxylase (AdoMetDC), a key regulated enzyme in the pathway of polyamine biosynthesis, is feedback-controlled at the level of translation by spermidine and spermine. Polyamines 101-110 adenosylmethionine decarboxylase 1 Homo sapiens 13-47 11489903-1 2001 Synthesis of S-adenosylmethionine decarboxylase (AdoMetDC), a key regulated enzyme in the pathway of polyamine biosynthesis, is feedback-controlled at the level of translation by spermidine and spermine. Polyamines 101-110 adenosylmethionine decarboxylase 1 Homo sapiens 49-57 11489903-2 2001 The peptide product of an upstream open reading frame (uORF) in the mRNA is solely responsible for polyamine regulation of AdoMetDC translation. Polyamines 99-108 adenosylmethionine decarboxylase 1 Homo sapiens 123-131 11489903-7 2001 These observations are consistent with a model in which regulation of ribosome pausing at the uORF by polyamines controls ribosome access to the downstream AdoMetDC reading frame. Polyamines 102-112 adenosylmethionine decarboxylase 1 Homo sapiens 156-164 11222959-2 2001 SAMDC is a key enzyme to synthesize polyamines that are known to be involved in a large array of biological events including protein synthesis, DNA stabilization, DNA replication, and cell proliferation. Polyamines 36-46 adenosylmethionine decarboxylase 1 Homo sapiens 0-5 11016654-1 2000 Cancer cells are known to display up-regulation of ornithine decarboxylase (ODC) and S-adenosylmethionine decarboxylase (AdoMetDC), the key enzymes in the biosynthesis of polyamines that are essential for cellular proliferation. Polyamines 171-181 adenosylmethionine decarboxylase 1 Homo sapiens 85-119 11163334-1 2001 Polyamine synthesis (by the action of ornithine decarboxylase [ODC] and S-adenosylmethionine decarboxylase [SAMDC]) and polyamine content are high in colon cancer. Polyamines 0-9 adenosylmethionine decarboxylase 1 Homo sapiens 72-106 11163334-1 2001 Polyamine synthesis (by the action of ornithine decarboxylase [ODC] and S-adenosylmethionine decarboxylase [SAMDC]) and polyamine content are high in colon cancer. Polyamines 0-9 adenosylmethionine decarboxylase 1 Homo sapiens 108-113 11076965-2 2000 Here we show that the overexpression of cDNA for S-adenosylmethionine decarboxylase (AdoMetDC), the main regulatory enzyme in the biosynthesis of higher polyamines, induces transformation of rodent fibroblasts when expressed in the sense or the antisense orientation. Polyamines 153-163 adenosylmethionine decarboxylase 1 Homo sapiens 49-83 11076965-2 2000 Here we show that the overexpression of cDNA for S-adenosylmethionine decarboxylase (AdoMetDC), the main regulatory enzyme in the biosynthesis of higher polyamines, induces transformation of rodent fibroblasts when expressed in the sense or the antisense orientation. Polyamines 153-163 adenosylmethionine decarboxylase 1 Homo sapiens 85-93 11016654-1 2000 Cancer cells are known to display up-regulation of ornithine decarboxylase (ODC) and S-adenosylmethionine decarboxylase (AdoMetDC), the key enzymes in the biosynthesis of polyamines that are essential for cellular proliferation. Polyamines 171-181 adenosylmethionine decarboxylase 1 Homo sapiens 121-129 10413038-1 1999 The gene for S-adenosylmethionine decarboxylase (AdoMetDC), a rate-limiting enzyme in the biosynthesis of polyamines, has been cloned from a Trypanosoma cruz cDNA library. Polyamines 106-116 adenosylmethionine decarboxylase 1 Homo sapiens 49-57 10944598-2 2000 SAM486A (CGP 48664) is a new inhibitor of the polyamine biosynthetic enzyme S-adenosylmethionine decarboxylase (SAMDC), more potent and specific than the first-generation SAMDC inhibitor methylglyoxal (bis) guanylhydrazone (MGBG). Polyamines 46-55 adenosylmethionine decarboxylase 1 Homo sapiens 76-110 10944598-2 2000 SAM486A (CGP 48664) is a new inhibitor of the polyamine biosynthetic enzyme S-adenosylmethionine decarboxylase (SAMDC), more potent and specific than the first-generation SAMDC inhibitor methylglyoxal (bis) guanylhydrazone (MGBG). Polyamines 46-55 adenosylmethionine decarboxylase 1 Homo sapiens 112-117 10944598-2 2000 SAM486A (CGP 48664) is a new inhibitor of the polyamine biosynthetic enzyme S-adenosylmethionine decarboxylase (SAMDC), more potent and specific than the first-generation SAMDC inhibitor methylglyoxal (bis) guanylhydrazone (MGBG). Polyamines 46-55 adenosylmethionine decarboxylase 1 Homo sapiens 171-176 10482374-5 1999 This coincided with inhibition of polyamine uptake and synthetic enzyme activities, with reduced ornithine decarboxylase (ODC) and S-adenosylmethionine decarboxylase (SAM-DC) but increased spermidine/spermine N1-acetyltransferase (SSAT) activities, as measured in DRO90-1 cells. Polyamines 34-43 adenosylmethionine decarboxylase 1 Homo sapiens 131-165 10378277-1 1999 BACKGROUND: S-Adenosylmethionine decarboxylase (AdoMetDC) is a critical regulatory enzyme of the polyamine synthetic pathway, and a well-studied drug target. Polyamines 97-106 adenosylmethionine decarboxylase 1 Homo sapiens 12-46 10228944-4 1999 In EGF-treated cells, peak activities of two key enzymes of polyamine biosynthesis, ornithine decarboxylase (ODC) and S-adenosylmethionine decarboxylase (SAMDC), were reduced by 57% and 83%, respectively. Polyamines 60-69 adenosylmethionine decarboxylase 1 Homo sapiens 118-152 10228944-4 1999 In EGF-treated cells, peak activities of two key enzymes of polyamine biosynthesis, ornithine decarboxylase (ODC) and S-adenosylmethionine decarboxylase (SAMDC), were reduced by 57% and 83%, respectively. Polyamines 60-69 adenosylmethionine decarboxylase 1 Homo sapiens 154-159 10378277-1 1999 BACKGROUND: S-Adenosylmethionine decarboxylase (AdoMetDC) is a critical regulatory enzyme of the polyamine synthetic pathway, and a well-studied drug target. Polyamines 97-106 adenosylmethionine decarboxylase 1 Homo sapiens 48-56 10216947-2 1999 The rate-limiting enzymes of the polyamine pathway, ornithine decarboxylase (ODC) and S-adenosylmethionine decarboxylase (AdoMetDC), are highly regulated in the cell, and much of this regulation occurs at the level of translation. Polyamines 33-42 adenosylmethionine decarboxylase 1 Homo sapiens 86-120 10216947-2 1999 The rate-limiting enzymes of the polyamine pathway, ornithine decarboxylase (ODC) and S-adenosylmethionine decarboxylase (AdoMetDC), are highly regulated in the cell, and much of this regulation occurs at the level of translation. Polyamines 33-42 adenosylmethionine decarboxylase 1 Homo sapiens 122-130 10216947-6 1999 The translation of both ODC and AdoMetDC is negatively regulated by intracellular changes in the polyamines spermidine and spermine. Polyamines 97-107 adenosylmethionine decarboxylase 1 Homo sapiens 32-40 10216947-7 1999 Thus, when polyamine levels are low, the synthesis of both ODC and AdoMetDC is increased, and an increase in polyamine content causes a corresponding decrease in protein synthesis. Polyamines 11-20 adenosylmethionine decarboxylase 1 Homo sapiens 67-75 10216947-9 1999 In contrast, the amino acid sequence that is encoded by the upstream ORF is critical for polyamine regulation of AdoMetDC synthesis and polyamines may affect synthesis by interaction with the putative peptide, MAGDIS. Polyamines 89-98 adenosylmethionine decarboxylase 1 Homo sapiens 113-121 9880821-11 1998 SAMDC might be a preferable target for therapeutic attempts to impair growth by reducing intracellular polyamine pools in colon cancer. Polyamines 103-112 adenosylmethionine decarboxylase 1 Homo sapiens 0-5 9225849-1 1997 S-adenosylmethionine decarboxylase (SAMDC; EC 4.1.4.50) is one of the key enzymes in polyamine biosynthesis, and the product of its catalytic reaction, decarboxylated S-adenosylmethionine (dcSAM), serves as an aminopropyl donor in the biosynthesis of spermidine and spermine. Polyamines 85-94 adenosylmethionine decarboxylase 1 Homo sapiens 0-34 9677309-2 1998 The parasites have instead been assumed to depend on putrescine uptake and S-adenosylmethionine decarboxylase (AdoMetDC) for their synthesis of the polyamines spermidine and spermine. Polyamines 148-158 adenosylmethionine decarboxylase 1 Homo sapiens 111-119 9743591-1 1998 The effects of CGP 48664 and DFMO, selective inhibitors of the key enzymes of polyamine biosynthesis, namely, of S-adenosylmethionine decarboxylase (AdoMetDC) and ornithine decarboxylase (ODC), were investigated on growth, polyamine metabolism, and DNA methylation in the Caco-2 cell line. Polyamines 78-87 adenosylmethionine decarboxylase 1 Homo sapiens 113-147 9743591-1 1998 The effects of CGP 48664 and DFMO, selective inhibitors of the key enzymes of polyamine biosynthesis, namely, of S-adenosylmethionine decarboxylase (AdoMetDC) and ornithine decarboxylase (ODC), were investigated on growth, polyamine metabolism, and DNA methylation in the Caco-2 cell line. Polyamines 78-87 adenosylmethionine decarboxylase 1 Homo sapiens 149-157 9225849-1 1997 S-adenosylmethionine decarboxylase (SAMDC; EC 4.1.4.50) is one of the key enzymes in polyamine biosynthesis, and the product of its catalytic reaction, decarboxylated S-adenosylmethionine (dcSAM), serves as an aminopropyl donor in the biosynthesis of spermidine and spermine. Polyamines 85-94 adenosylmethionine decarboxylase 1 Homo sapiens 36-41 8905633-0 1996 Regulation of ornithine decarboxylase and S-adenosylmethionine decarboxylase in a polyamine auxotrophic cell line. Polyamines 82-91 adenosylmethionine decarboxylase 1 Homo sapiens 42-76 8939886-0 1996 The upstream open reading frame of the mRNA encoding S-adenosylmethionine decarboxylase is a polyamine-responsive translational control element. Polyamines 93-102 adenosylmethionine decarboxylase 1 Homo sapiens 53-87 8939886-1 1996 S-Adenosylmethionine decarboxylase (AdoMetDC) is a key enzyme in the pathway of polyamine biosynthesis. Polyamines 80-89 adenosylmethionine decarboxylase 1 Homo sapiens 0-34 8939886-1 1996 S-Adenosylmethionine decarboxylase (AdoMetDC) is a key enzyme in the pathway of polyamine biosynthesis. Polyamines 80-89 adenosylmethionine decarboxylase 1 Homo sapiens 36-44 8905633-6 1996 The synthesis of S-adenosylmethionine decarboxylase (AdoMetDC) was also increased in the cells seeded in the absence of polyamines. Polyamines 120-130 adenosylmethionine decarboxylase 1 Homo sapiens 17-51 8905633-6 1996 The synthesis of S-adenosylmethionine decarboxylase (AdoMetDC) was also increased in the cells seeded in the absence of polyamines. Polyamines 120-130 adenosylmethionine decarboxylase 1 Homo sapiens 53-61 7640515-1 1995 CGP 48664A (4-amidinoindan-1-one2"-amidinohydrazone) is a novel inhibitor of S-adenosyl-methionine decarboxylase (SAMDC), a key enzyme in the biosynthesis of polyamines, which are themselves essential for proliferation of mammalian cells. Polyamines 158-168 adenosylmethionine decarboxylase 1 Homo sapiens 77-112 8877009-1 1996 SAMDC is a key enzyme in the biosynthesis of spermidine and spermine, 2 polyamines that are essential for cell proliferation. Polyamines 72-82 adenosylmethionine decarboxylase 1 Homo sapiens 0-5 7634128-12 1995 It can be concluded that antibodies to recombinant human AdoMetDC provide a tool for the immunohistochemical localization of AdoMetDC, and that the distribution of the enzyme in the tissues studied gives further support to the importance of polyamines in the development and functions of these organs. Polyamines 241-251 adenosylmethionine decarboxylase 1 Homo sapiens 57-65 7640515-1 1995 CGP 48664A (4-amidinoindan-1-one2"-amidinohydrazone) is a novel inhibitor of S-adenosyl-methionine decarboxylase (SAMDC), a key enzyme in the biosynthesis of polyamines, which are themselves essential for proliferation of mammalian cells. Polyamines 158-168 adenosylmethionine decarboxylase 1 Homo sapiens 114-119 7883014-1 1995 S-Adenosyl-L-methionine decarboxylases (AdoMetDC) are pyruvoyl-dependent enzymes producing the aminopropyl group for spermidine biosynthesis, and this reaction is the rate-limiting step in polyamine biosynthesis. Polyamines 189-198 adenosylmethionine decarboxylase 1 Homo sapiens 40-48 7599326-2 1995 This effect was accompanied by a significant increase of the activity of two key enzymes of the polyamine pathway, i.e. ornithine decarboxylase (ODC) and S-adenosylmethionine decarboxylase (SAMDC). Polyamines 96-105 adenosylmethionine decarboxylase 1 Homo sapiens 154-188 7599326-2 1995 This effect was accompanied by a significant increase of the activity of two key enzymes of the polyamine pathway, i.e. ornithine decarboxylase (ODC) and S-adenosylmethionine decarboxylase (SAMDC). Polyamines 96-105 adenosylmethionine decarboxylase 1 Homo sapiens 190-195 7945201-1 1994 S-Adenosylmethionine decarboxylase (AdoMetDC), a rate-limiting enzyme in polyamine biosynthesis, is regulated by polyamines at the levels of both transcription and translation. Polyamines 73-82 adenosylmethionine decarboxylase 1 Homo sapiens 0-34 7999790-1 1995 Mammalian S-adenosylmethionine decarboxylase (AdoMetDC), which catalyzes a key step in the biosynthesis of polyamines, is regulated by a multitude of mechanisms. Polyamines 107-117 adenosylmethionine decarboxylase 1 Homo sapiens 10-44 7999790-1 1995 Mammalian S-adenosylmethionine decarboxylase (AdoMetDC), which catalyzes a key step in the biosynthesis of polyamines, is regulated by a multitude of mechanisms. Polyamines 107-117 adenosylmethionine decarboxylase 1 Homo sapiens 46-54 7999790-8 1995 The high expression of AdoMetDC was reflected in a marked change in intracellular polyamine levels. Polyamines 82-91 adenosylmethionine decarboxylase 1 Homo sapiens 23-31 7999790-12 1995 The effects on the expression of AdoMetDC of polyamine synthesis inhibitors varied dependent on whether the COS cells were transfected with control vector or pSDC:16, in spite of similar effects on cellular polyamine levels, indicating a difference in feedback regulation of "native" and recombinant AdoMetDC. Polyamines 45-54 adenosylmethionine decarboxylase 1 Homo sapiens 33-41 7999790-12 1995 The effects on the expression of AdoMetDC of polyamine synthesis inhibitors varied dependent on whether the COS cells were transfected with control vector or pSDC:16, in spite of similar effects on cellular polyamine levels, indicating a difference in feedback regulation of "native" and recombinant AdoMetDC. Polyamines 45-54 adenosylmethionine decarboxylase 1 Homo sapiens 300-308 7789170-1 1995 S-adenosylmethionine decarboxylase (AdoMet-DC) is a key enzyme in polyamine biosynthesis. Polyamines 66-75 adenosylmethionine decarboxylase 1 Homo sapiens 0-34 7789170-1 1995 S-adenosylmethionine decarboxylase (AdoMet-DC) is a key enzyme in polyamine biosynthesis. Polyamines 66-75 adenosylmethionine decarboxylase 1 Homo sapiens 36-45 7945201-1 1994 S-Adenosylmethionine decarboxylase (AdoMetDC), a rate-limiting enzyme in polyamine biosynthesis, is regulated by polyamines at the levels of both transcription and translation. Polyamines 73-82 adenosylmethionine decarboxylase 1 Homo sapiens 36-44 7945201-1 1994 S-Adenosylmethionine decarboxylase (AdoMetDC), a rate-limiting enzyme in polyamine biosynthesis, is regulated by polyamines at the levels of both transcription and translation. Polyamines 113-123 adenosylmethionine decarboxylase 1 Homo sapiens 0-34 7945201-1 1994 S-Adenosylmethionine decarboxylase (AdoMetDC), a rate-limiting enzyme in polyamine biosynthesis, is regulated by polyamines at the levels of both transcription and translation. Polyamines 113-123 adenosylmethionine decarboxylase 1 Homo sapiens 36-44 8142949-0 1994 Expression of a human S-adenosylmethionine decarboxylase cDNA in transgenic tobacco and its effects on polyamine biosynthesis. Polyamines 103-112 adenosylmethionine decarboxylase 1 Homo sapiens 22-56 8205541-1 1994 Inhibitors of the polyamine biosynthetic enzyme S-adenosylmethionine decarboxylase (SAMDC), derived from methylglyoxal-bis(guanylhydrazone) (MGBG), have been shown to have significant antitumor activity in several human solid tumor systems (U. Regenass et al., Cancer Res., 52:4712-4718, 1992). Polyamines 18-27 adenosylmethionine decarboxylase 1 Homo sapiens 48-82 8205541-1 1994 Inhibitors of the polyamine biosynthetic enzyme S-adenosylmethionine decarboxylase (SAMDC), derived from methylglyoxal-bis(guanylhydrazone) (MGBG), have been shown to have significant antitumor activity in several human solid tumor systems (U. Regenass et al., Cancer Res., 52:4712-4718, 1992). Polyamines 18-27 adenosylmethionine decarboxylase 1 Homo sapiens 84-89 8142949-1 1994 S-adenosylmethionine decarboxylase (SAMDC; EC 4.1.1.50) is a key regulatory enzyme in the polyamine biosynthetic pathway. Polyamines 90-99 adenosylmethionine decarboxylase 1 Homo sapiens 0-34 8142949-1 1994 S-adenosylmethionine decarboxylase (SAMDC; EC 4.1.1.50) is a key regulatory enzyme in the polyamine biosynthetic pathway. Polyamines 90-99 adenosylmethionine decarboxylase 1 Homo sapiens 36-41 8142949-3 1994 In order to gain more insight into the role of polyamines in plants, human SAMDC cDNA under control of 35S promoter of cauliflower mosaic virus, along with a neomycin phosphotransferase gene, was transferred to tobacco (Nicotiana tabacum cv.Xanthi) via Agrobacterium tumefaciens. Polyamines 47-57 adenosylmethionine decarboxylase 1 Homo sapiens 75-80 8280812-2 1993 The drop in cell numbers after 24 h incubation with increasing concentrations of TGF-beta 1 (0.01, 0.1, 1.0, 10.0 ng/ml) was accompanied by significant suppression of the activity of two key enzymes of polyamine biosynthesis: ornithine decarboxylase (ODC) and S-adenosylmethionine decarboxylase (SAMDC). Polyamines 202-211 adenosylmethionine decarboxylase 1 Homo sapiens 260-294 8280812-2 1993 The drop in cell numbers after 24 h incubation with increasing concentrations of TGF-beta 1 (0.01, 0.1, 1.0, 10.0 ng/ml) was accompanied by significant suppression of the activity of two key enzymes of polyamine biosynthesis: ornithine decarboxylase (ODC) and S-adenosylmethionine decarboxylase (SAMDC). Polyamines 202-211 adenosylmethionine decarboxylase 1 Homo sapiens 296-301 8280812-4 1993 We suppose that the lack of an evident drop in concentration of spermidine and spermine in spite of a significant decrease in ODC and SAMDC activity in K 562 cells exposed to TGF-beta 1 resulted from the uptake of polyamines from the extracellular space. Polyamines 214-224 adenosylmethionine decarboxylase 1 Homo sapiens 134-139 8361629-1 1993 We measured the activity of S-adenosylmethionine decarboxylase (SAMDC), a key regulatory enzyme of polyamine biosynthesis, in autopsied brain from 13 patients with Alzheimer"s Disease (AD). Polyamines 99-108 adenosylmethionine decarboxylase 1 Homo sapiens 28-62 8319678-0 1993 Polyamine-mediated regulation of S-adenosylmethionine decarboxylase expression in mammalian cells. Polyamines 0-9 adenosylmethionine decarboxylase 1 Homo sapiens 33-67 8353934-3 1993 In order to provide baseline information, in normal human brain, on one of the key polyamine synthesising enzymes, S-adenosylmethionine decarboxylase (SAMDC), we examined the sensitivity of this enzyme to various cofactors/inhibitors, its regional distribution, and influence of aging in neurologically normal autopsied human brain. Polyamines 83-92 adenosylmethionine decarboxylase 1 Homo sapiens 115-149 8353934-3 1993 In order to provide baseline information, in normal human brain, on one of the key polyamine synthesising enzymes, S-adenosylmethionine decarboxylase (SAMDC), we examined the sensitivity of this enzyme to various cofactors/inhibitors, its regional distribution, and influence of aging in neurologically normal autopsied human brain. Polyamines 83-92 adenosylmethionine decarboxylase 1 Homo sapiens 151-156 8353934-8 1993 Since SAMDC is a key regulatory enzyme in the synthesis of spermidine and spermine, the marked increase in SAMDC activity in the neonate and the sustained high enzyme levels throughout adulthood, imply a role for these polyamines in both development and mature brain function. Polyamines 219-229 adenosylmethionine decarboxylase 1 Homo sapiens 6-11 8361629-1 1993 We measured the activity of S-adenosylmethionine decarboxylase (SAMDC), a key regulatory enzyme of polyamine biosynthesis, in autopsied brain from 13 patients with Alzheimer"s Disease (AD). Polyamines 99-108 adenosylmethionine decarboxylase 1 Homo sapiens 64-69 8361629-4 1993 Above-normal SAMDC activity implies increased levels/metabolism of spermidine and spermine, two polyamines which are involved in neuronal regeneration, growth factor production, and activation of excitatory N-methyl-D-aspartate preferring glutamate receptors. Polyamines 96-106 adenosylmethionine decarboxylase 1 Homo sapiens 13-18 1463454-0 1992 Regulation of S-adenosylmethionine decarboxylase activity by alterations in the intracellular polyamine content. Polyamines 94-103 adenosylmethionine decarboxylase 1 Homo sapiens 14-48 1463454-2 1992 AdoMetDC levels were inversely related to the polyamine content, and spermine was the more potent repressor of AdoMetDC activity, but only spermidine affected the amount of AdoMetDC mRNA. Polyamines 46-55 adenosylmethionine decarboxylase 1 Homo sapiens 0-8 1358085-1 1992 Biosynthesis of the polyamines spermidine and spermine and their precursor putrescine is controlled by the activity of the two key enzymes ornithine decarboxylase (ODC) and S-adenosylmethionine decarboxylase (SAMDC). Polyamines 20-30 adenosylmethionine decarboxylase 1 Homo sapiens 173-207 1358085-1 1992 Biosynthesis of the polyamines spermidine and spermine and their precursor putrescine is controlled by the activity of the two key enzymes ornithine decarboxylase (ODC) and S-adenosylmethionine decarboxylase (SAMDC). Polyamines 20-30 adenosylmethionine decarboxylase 1 Homo sapiens 209-214 1562452-1 1992 Synthesis of the polyamines putrescine, spermidine, and spermine is controlled by the activity of the key enzymes ornithine decarboxylase (ODC) and S-adenosylmethionine decarboxylase (SAMDC). Polyamines 17-27 adenosylmethionine decarboxylase 1 Homo sapiens 148-182 1562452-1 1992 Synthesis of the polyamines putrescine, spermidine, and spermine is controlled by the activity of the key enzymes ornithine decarboxylase (ODC) and S-adenosylmethionine decarboxylase (SAMDC). Polyamines 17-27 adenosylmethionine decarboxylase 1 Homo sapiens 184-189 1562452-3 1992 Reversible cerebral ischemia triggers pathological disturbances in polyamine metabolism that are characterized by a sharp increase in ODC synthesis, even in the most vulnerable hippocampal CA1 subfield in which overall protein synthesis is severely depressed at the same time, and a marked suppression of SAMDC synthesis in parallel with the inhibition of overall protein synthesis. Polyamines 67-76 adenosylmethionine decarboxylase 1 Homo sapiens 305-310 1301596-4 1992 Therefore, S-adenosylmethionine decarboxylase (AdoMetDC, EC 4.1.1.50) is essential for polyamine synthesis. Polyamines 87-96 adenosylmethionine decarboxylase 1 Homo sapiens 11-45 1301596-4 1992 Therefore, S-adenosylmethionine decarboxylase (AdoMetDC, EC 4.1.1.50) is essential for polyamine synthesis. Polyamines 87-96 adenosylmethionine decarboxylase 1 Homo sapiens 47-55 1301596-7 1992 This review describes the current state of knowledge of the structure and properties of AdoMetDC, the available inhibitors of this enzyme, their mechanism of action and their effects on polyamines and on the growth of tumors and protozoan parasites. Polyamines 186-196 adenosylmethionine decarboxylase 1 Homo sapiens 88-96 19997761-1 2010 S-adenosylmethionine decarboxylase (AdoMetDC) is a critical enzyme in the polyamine biosynthetic pathway and a subject of many structural and biochemical investigations for anti-cancer and anti-parasitic therapy. Polyamines 74-83 adenosylmethionine decarboxylase 1 Homo sapiens 0-34 19997761-1 2010 S-adenosylmethionine decarboxylase (AdoMetDC) is a critical enzyme in the polyamine biosynthetic pathway and a subject of many structural and biochemical investigations for anti-cancer and anti-parasitic therapy. Polyamines 74-83 adenosylmethionine decarboxylase 1 Homo sapiens 36-44 34420674-3 2021 (2021) report that keratinocyte differentiation requires a shift in polyamine ratios that is mediated by AMD1. Polyamines 68-77 adenosylmethionine decarboxylase 1 Homo sapiens 105-109