Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
2001-2-5
pubmed:abstractText
Recently isolated at Merck, apicidin inhibits both mammalian and protozoan histone deacetylases (HDACs). The conversion of apicidin, a nonselective nanomolar inhibitor of HDACs, into a series of picomolar indole-modified and parasite-selective tryptophan-replacement analogues is described within this structure-activity study.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jan
pubmed:issn
0960-894X
pubmed:author
pubmed:issnType
Print
pubmed:day
22
pubmed:volume
11
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
113-7
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed-meshheading:11206439-Animals, pubmed-meshheading:11206439-Antiprotozoal Agents, pubmed-meshheading:11206439-Biological Factors, pubmed-meshheading:11206439-Cattle, pubmed-meshheading:11206439-Cell Division, pubmed-meshheading:11206439-Cell Line, pubmed-meshheading:11206439-Combinatorial Chemistry Techniques, pubmed-meshheading:11206439-Eimeria tenella, pubmed-meshheading:11206439-Enzyme Inhibitors, pubmed-meshheading:11206439-Fusarium, pubmed-meshheading:11206439-HeLa Cells, pubmed-meshheading:11206439-Histone Deacetylase Inhibitors, pubmed-meshheading:11206439-Humans, pubmed-meshheading:11206439-Indoles, pubmed-meshheading:11206439-Microbial Sensitivity Tests, pubmed-meshheading:11206439-Peptides, Cyclic, pubmed-meshheading:11206439-Plasmodium falciparum, pubmed-meshheading:11206439-Structure-Activity Relationship, pubmed-meshheading:11206439-Tryptophan
pubmed:year
2001
pubmed:articleTitle
Broad spectrum antiprotozoal agents that inhibit histone deacetylase: structure-activity relationships of apicidin. Part 2.
pubmed:affiliation
Merck Research Laboratories, Merck & Co., Inc., Rahway, NJ 07065, USA. steve_colletti@merck.com
pubmed:publicationType
Journal Article