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pubmed-article:19362833pubmed:abstractTextThe inhibitory activity of base-modified SAH analogues and the specificity of inhibiting human DNMT1 and DNMT3b2 enzymes was explored. The 6-amino group was essential while the 7-N of the adenine ring of SAH could be replaced by CH- without loss of activity against both enzymes. The introduction of small groups at the 2-position of the adenine moiety favors DNMT1 over DNMT3b2 inhibition whereas alkylation of the N(6)-amino moiety favors the inhibition of DNMT3b2 enzyme.lld:pubmed
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pubmed-article:19362833pubmed:articleTitleSAR around (l)-S-adenosyl-l-homocysteine, an inhibitor of human DNA methyltransferase (DNMT) enzymes.lld:pubmed
pubmed-article:19362833pubmed:affiliationMethylGene Inc., Departments of Medicinal Chemistry, Montreal, Quebec, Canada.lld:pubmed
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