Source:http://linkedlifedata.com/resource/pubmed/id/19362833
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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
10
|
| pubmed:dateCreated |
2009-5-4
|
| pubmed:abstractText |
The 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.
|
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical | |
| pubmed:status |
MEDLINE
|
| pubmed:month |
May
|
| pubmed:issn |
1464-3405
|
| pubmed:author |
pubmed-author:BeaulieuNormanN,
pubmed-author:BernsteinNaomyN,
pubmed-author:BestermanJeffrey MJM,
pubmed-author:ClaridgeStephenS,
pubmed-author:DelormeDanielD,
pubmed-author:EloweNadineN,
pubmed-author:IsakovicLjubomirL,
pubmed-author:LlewellynDavid BDB,
pubmed-author:MacLeodA RobertAR,
pubmed-author:PetschnerAndrea JAJ,
pubmed-author:RaeppelFranckF,
pubmed-author:RahilJubrailJ,
pubmed-author:SaavedraOscar MOM,
pubmed-author:VaisburgArkadiiA,
pubmed-author:WahhabAmalA,
pubmed-author:ZhanLijieL
|
| pubmed:issnType |
Electronic
|
| pubmed:day |
15
|
| pubmed:volume |
19
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
2747-51
|
| pubmed:meshHeading | |
| pubmed:year |
2009
|
| pubmed:articleTitle |
SAR around (l)-S-adenosyl-l-homocysteine, an inhibitor of human DNA methyltransferase (DNMT) enzymes.
|
| pubmed:affiliation |
MethylGene Inc., Departments of Medicinal Chemistry, Montreal, Quebec, Canada.
|
| pubmed:publicationType |
Journal Article
|