PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 20215859-6 2010 The expression levels of spermine anabolic enzymes: ornithine decarboxylase (ODC1) and S-adenosylmethionine decarboxylase (AMD1) in benign epithelia surrounding cancer glands was logarithmically reduced with the increase of Vpsa (ODC1, p < 0.016; AMD1, p < 0.048), and antizyme (OAZ1) expression in cancer cells was increased with the increase of Vpsa (p < 0.001). Spermine 25-33 adenosylmethionine decarboxylase 1 Homo sapiens 123-127 22391449-4 2012 Overexpression of Amd1 or addition of the polyamine spermine blocks ESC-to-NPC conversion, suggesting Amd1 must be down-regulated to decrease the levels of inhibitory spermine during differentiation. Spermine 52-60 adenosylmethionine decarboxylase 1 Homo sapiens 102-106 22391449-4 2012 Overexpression of Amd1 or addition of the polyamine spermine blocks ESC-to-NPC conversion, suggesting Amd1 must be down-regulated to decrease the levels of inhibitory spermine during differentiation. Spermine 167-175 adenosylmethionine decarboxylase 1 Homo sapiens 18-22 20215859-6 2010 The expression levels of spermine anabolic enzymes: ornithine decarboxylase (ODC1) and S-adenosylmethionine decarboxylase (AMD1) in benign epithelia surrounding cancer glands was logarithmically reduced with the increase of Vpsa (ODC1, p < 0.016; AMD1, p < 0.048), and antizyme (OAZ1) expression in cancer cells was increased with the increase of Vpsa (p < 0.001). Spermine 25-33 adenosylmethionine decarboxylase 1 Homo sapiens 250-254 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. Spermine 164-172 adenosylmethionine decarboxylase 1 Homo sapiens 48-56 17593800-1 2007 S-adenosylmethionine decarboxylase (SAMDC) is an essential enzyme for the synthesis of spermidine and spermine in the biosynthetic pathway of polyamines. Spermine 102-110 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. Spermine 102-110 adenosylmethionine decarboxylase 1 Homo sapiens 36-41 16941339-2 2006 The pharmaceutical interference with SAMDC activity results in the depletion of the intracellular pool of spermidine and spermine. Spermine 121-129 adenosylmethionine decarboxylase 1 Homo sapiens 37-42 16515461-1 2006 S-adenosylmethionine decarboxylase (AdoMetDC) is a key enzyme in the biosynthesis of the polyamines spermidine and spermine. Spermine 115-123 adenosylmethionine decarboxylase 1 Homo sapiens 0-34 15965903-9 2006 Pre-treatment with CGP 48664, an S-adenosylmethionine decarboxylase (SAMDC) inhibitor markedly reduced spermidine and spermine levels, and provoked effects similar to those caused by DFMO. Spermine 118-126 adenosylmethionine decarboxylase 1 Homo sapiens 33-67 15965903-9 2006 Pre-treatment with CGP 48664, an S-adenosylmethionine decarboxylase (SAMDC) inhibitor markedly reduced spermidine and spermine levels, and provoked effects similar to those caused by DFMO. Spermine 118-126 adenosylmethionine decarboxylase 1 Homo sapiens 69-74 16515461-1 2006 S-adenosylmethionine decarboxylase (AdoMetDC) is a key enzyme in the biosynthesis of the polyamines spermidine and spermine. Spermine 115-123 adenosylmethionine decarboxylase 1 Homo sapiens 36-44 16515461-3 2006 AdoMetDC catalyzes decarboxylation of S-adenosylmethionine (AdoMet) which provides aminopropyl groups for spermidine and spermine synthesis. Spermine 121-129 adenosylmethionine decarboxylase 1 Homo sapiens 0-8 10216947-6 1999 The translation of both ODC and AdoMetDC is negatively regulated by intracellular changes in the polyamines spermidine and spermine. Spermine 123-131 adenosylmethionine decarboxylase 1 Homo sapiens 32-40 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. Spermine 179-187 adenosylmethionine decarboxylase 1 Homo sapiens 36-44 15821146-4 2005 This sequence may help to keep the transcript of its downstream cistron at a relatively low level and function together with its own promoter in response to external stimuli or internal changes of spermidine and spermine to initiate and regulate SAMDC expression. Spermine 212-220 adenosylmethionine decarboxylase 1 Homo sapiens 246-251 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. Spermine 166-174 adenosylmethionine decarboxylase 1 Homo sapiens 4-12 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. Spermine 190-198 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. Spermine 190-198 adenosylmethionine decarboxylase 1 Homo sapiens 36-44 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. Spermine 194-202 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. Spermine 194-202 adenosylmethionine decarboxylase 1 Homo sapiens 49-57 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. Spermine 191-199 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. Spermine 191-199 adenosylmethionine decarboxylase 1 Homo sapiens 59-67 9743591-3 1998 In the presence of the AdoMetDC inhibitor, ODC activity and the intracellular pool of putrescine were enhanced, whereas the spermidine and spermine pools were decreased. Spermine 139-147 adenosylmethionine decarboxylase 1 Homo sapiens 23-31 7656236-4 1995 Since SAMDC-overexpressing clones exhibited increased clonogenicity in soft agar, our data suggest that spermine may be selectively involved in conferring a more invasive phenotype to breast cancer cells. Spermine 104-112 adenosylmethionine decarboxylase 1 Homo sapiens 6-11 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. Spermine 266-274 adenosylmethionine decarboxylase 1 Homo sapiens 0-34 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. Spermine 266-274 adenosylmethionine decarboxylase 1 Homo sapiens 36-41 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. Spermine 174-182 adenosylmethionine decarboxylase 1 Homo sapiens 111-119 8877009-1 1996 SAMDC is a key enzyme in the biosynthesis of spermidine and spermine, 2 polyamines that are essential for cell proliferation. Spermine 60-68 adenosylmethionine decarboxylase 1 Homo sapiens 0-5 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. Spermine 74-82 adenosylmethionine decarboxylase 1 Homo sapiens 6-11 7945201-0 1994 Role of the 5"-untranslated region of mRNA in the synthesis of S-adenosylmethionine decarboxylase and its regulation by spermine. Spermine 120-128 adenosylmethionine decarboxylase 1 Homo sapiens 63-97 8395844-7 1993 The reduction of spermine produced by BDAP led to a substantial increase in the activity of S-adenosylmethionine decarboxylase (AdoMetDC) showing that the repression of this enzyme by spermine is greater than the repression by spermidine. Spermine 17-25 adenosylmethionine decarboxylase 1 Homo sapiens 92-126 8395844-7 1993 The reduction of spermine produced by BDAP led to a substantial increase in the activity of S-adenosylmethionine decarboxylase (AdoMetDC) showing that the repression of this enzyme by spermine is greater than the repression by spermidine. Spermine 17-25 adenosylmethionine decarboxylase 1 Homo sapiens 128-136 8395844-7 1993 The reduction of spermine produced by BDAP led to a substantial increase in the activity of S-adenosylmethionine decarboxylase (AdoMetDC) showing that the repression of this enzyme by spermine is greater than the repression by spermidine. Spermine 184-192 adenosylmethionine decarboxylase 1 Homo sapiens 92-126 8395844-7 1993 The reduction of spermine produced by BDAP led to a substantial increase in the activity of S-adenosylmethionine decarboxylase (AdoMetDC) showing that the repression of this enzyme by spermine is greater than the repression by spermidine. Spermine 184-192 adenosylmethionine decarboxylase 1 Homo sapiens 128-136 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). Spermine 56-64 adenosylmethionine decarboxylase 1 Homo sapiens 148-182 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. Spermine 82-90 adenosylmethionine decarboxylase 1 Homo sapiens 13-18 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. Spermine 69-77 adenosylmethionine decarboxylase 1 Homo sapiens 111-119 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. Spermine 69-77 adenosylmethionine decarboxylase 1 Homo sapiens 111-119 1463454-3 1992 Transfection of COS-7 cells or CHO cells with plasmid constructs containing a chloramphenicol acetyltransferase (CAT) reporter gene driven by portions of the AdoMetDC promoter region indicated that CAT expression was altered by spermidine, but not by spermine, suggesting that there is a spermidine-responsive element in this promoter. Spermine 251-259 adenosylmethionine decarboxylase 1 Homo sapiens 158-166 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). Spermine 46-54 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). Spermine 46-54 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). Spermine 56-64 adenosylmethionine decarboxylase 1 Homo sapiens 184-189 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. Spermine 192-200 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. Spermine 192-200 adenosylmethionine decarboxylase 1 Homo sapiens 123-131 2775206-6 1989 This increase appears to be unrelated to the decrease in spermine content, because a similar rise in AdoMetDC activity was obtained when AdoDATO was given in addition to MMTA, in which case the spermine content remained largely unchanged. Spermine 194-202 adenosylmethionine decarboxylase 1 Homo sapiens 101-109 33783988-1 2021 BACKGROUND: S-adenosylmethionine decarboxylase proenzyme (AMD1) is a key enzyme involved in the synthesis of spermine (SPM) and spermidine (SPD), which are associated with multifarious cellular processes. Spermine 109-117 adenosylmethionine decarboxylase 1 Homo sapiens 58-62 33984347-0 2021 The polyamine regulator AMD1 up-regulates spermine levels to drive epidermal differentiation. Spermine 42-50 adenosylmethionine decarboxylase 1 Homo sapiens 24-28 33984347-5 2021 During keratinocyte differentiation, elevated AMD1 promotes decreased putrescine and increased spermine levels. Spermine 95-103 adenosylmethionine decarboxylase 1 Homo sapiens 46-50 33984347-6 2021 Knockdown/inhibition of AMD1 results in reduced spermine levels and inhibition of keratinocyte differentiation. Spermine 48-56 adenosylmethionine decarboxylase 1 Homo sapiens 24-28 33984347-7 2021 Supplementing AMD1-knockdown keratinocytes with exogenous spermidine/spermine rescued aberrant differentiation. Spermine 69-77 adenosylmethionine decarboxylase 1 Homo sapiens 14-18 32218733-4 2020 During the synthesis of spermidine and spermine, an amino-propyl group is provided by decarboxylated S-adenosylmethionine, and the latter is generated from S-adenosylmethionine by AdoMetDC (AdoMet decarboxylase). Spermine 39-47 adenosylmethionine decarboxylase 1 Homo sapiens 190-210 29906410-5 2018 Knockdown of AMD1 with small hairpin RNAs causes a delay in cell migration that is rescued by the addition of spermine. Spermine 110-118 adenosylmethionine decarboxylase 1 Homo sapiens 13-17