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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
7
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pubmed:dateCreated |
2010-3-22
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pubmed:abstractText |
Prototype inhibitors of protein arginine methyltransferases (PRMTs) have been constructed by attaching guanidine functionality via a variable linker to non-reactive amine analogues of the cellular co-factor (S)-adenosyl methionine (AdoMet). Potent inhibition of PRMT1 (IC(50) of approximately 3-6 microM) combined with weak inhibition of the lysine methyltransferase SET7 (approximately 50% of activity at 100 microM) was observed for two such compounds.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Apr
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pubmed:issn |
1464-3405
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pubmed:author |
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pubmed:copyrightInfo |
2010 Elsevier Ltd. All rights reserved.
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pubmed:issnType |
Electronic
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pubmed:day |
1
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pubmed:volume |
20
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
2103-5
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pubmed:meshHeading |
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pubmed:year |
2010
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pubmed:articleTitle |
Toward the development of potent and selective bisubstrate inhibitors of protein arginine methyltransferases.
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pubmed:affiliation |
School of Chemistry, University Park, University of Nottingham, Nottingham, NG7 2RD, UK. james.dowden@nottingham.ac.uk
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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