rdf:type |
|
lifeskim:mentions |
|
pubmed:issue |
10
|
pubmed:dateCreated |
2011-5-19
|
pubmed:abstractText |
We report the design and concise synthesis, in two steps from commercially available material, of novel, bioactive derivatives of the enzyme cofactor nicotinamide adenine dinucleotide (NAD). The new synthetic dinucleotides act as sirtuin (SIRT) inhibitors and show isoform selectivity for SIRT2 over SIRT1. An NMR-based conformational analysis suggests that the conformational preferences of individual analogues may contribute to their isoform selectivity.
|
pubmed:language |
eng
|
pubmed:journal |
|
pubmed:citationSubset |
IM
|
pubmed:chemical |
|
pubmed:status |
MEDLINE
|
pubmed:month |
May
|
pubmed:issn |
1520-4804
|
pubmed:author |
|
pubmed:issnType |
Electronic
|
pubmed:day |
26
|
pubmed:volume |
54
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
3492-9
|
pubmed:meshHeading |
pubmed-meshheading:21528845-Chemistry, Pharmaceutical,
pubmed-meshheading:21528845-Drug Design,
pubmed-meshheading:21528845-Humans,
pubmed-meshheading:21528845-Hydrogen Bonding,
pubmed-meshheading:21528845-Magnetic Resonance Spectroscopy,
pubmed-meshheading:21528845-Models, Chemical,
pubmed-meshheading:21528845-NAD,
pubmed-meshheading:21528845-Oxidation-Reduction,
pubmed-meshheading:21528845-Protein Binding,
pubmed-meshheading:21528845-Protein Conformation,
pubmed-meshheading:21528845-Protein Isoforms,
pubmed-meshheading:21528845-Recombinant Fusion Proteins,
pubmed-meshheading:21528845-Sirtuin 1,
pubmed-meshheading:21528845-Sirtuin 2
|
pubmed:year |
2011
|
pubmed:articleTitle |
Two-step synthesis of novel, bioactive derivatives of the ubiquitous cofactor nicotinamide adenine dinucleotide (NAD).
|
pubmed:affiliation |
School of Pharmacy, University of East Anglia, Norwich, NR4 7TJ, UK.
|
pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|