Title : Inhibition of S-adenosylmethionine decarboxylase by inhibitor SAM486A connects polyamine metabolism with p53-Mdm2-Akt/protein kinase B regulation and apoptosis in neuroblastoma.

Pub. Date : 2009 Jul

PMID : 19584241






7 Functional Relationships(s)
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Protein Name
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1 Inhibition of S-adenosylmethionine decarboxylase by inhibitor SAM486A connects polyamine metabolism with p53-Mdm2-Akt/protein kinase B regulation and apoptosis in neuroblastoma. Polyamines adenosylmethionine decarboxylase 1 Homo sapiens
2 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 adenosylmethionine decarboxylase 1 Homo sapiens
3 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 adenosylmethionine decarboxylase 1 Homo sapiens
4 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 adenosylmethionine decarboxylase 1 Homo sapiens
5 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 adenosylmethionine decarboxylase 1 Homo sapiens
6 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 adenosylmethionine decarboxylase 1 Homo sapiens
7 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 adenosylmethionine decarboxylase 1 Homo sapiens