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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
18
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pubmed:dateCreated |
2001-8-31
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pubmed:abstractText |
[structure: see text]. Isolation and structure elucidation of two novel cyclic tetrapeptides that show a variety of potent antiprotozoal activities by reversibly inhibiting HDAC have been reported. These are the new members of a unique family of cyclic tetrapeptides that do not require the electrophilic alpha-epoxyketone moiety of HC-toxin, trapoxin A, or chlamydocin for their potent activities against HDAC and the malarial parasite.
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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 |
Sep
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pubmed:issn |
1523-7060
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
6
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pubmed:volume |
3
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
2815-8
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:11529764-Amino Acid Substitution,
pubmed-meshheading:11529764-Animals,
pubmed-meshheading:11529764-Antiprotozoal Agents,
pubmed-meshheading:11529764-Eimeria tenella,
pubmed-meshheading:11529764-Histone Deacetylase Inhibitors,
pubmed-meshheading:11529764-Histone Deacetylases,
pubmed-meshheading:11529764-Magnetic Resonance Spectroscopy,
pubmed-meshheading:11529764-Molecular Conformation,
pubmed-meshheading:11529764-Parasitic Sensitivity Tests,
pubmed-meshheading:11529764-Peptides, Cyclic,
pubmed-meshheading:11529764-Proline,
pubmed-meshheading:11529764-Sarcocystidae,
pubmed-meshheading:11529764-Valine
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pubmed:year |
2001
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pubmed:articleTitle |
Structure, histone deacetylase, and antiprotozoal activities of apicidins B and C, congeners of apicidin with proline and valine substitutions.
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pubmed:affiliation |
Merck Research Laboratories, RY80Y-355, P.O. Box 2000, Rahway, New Jersey 07065, USA. sheo_singh@merck.com
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pubmed:publicationType |
Journal Article
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