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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
10
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pubmed:dateCreated |
1999-1-25
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pubmed:abstractText |
In order to establish structural elements responsible for inhibition of trypanothione reductase (TR) from Trypanosoma cruzi by 2-aminodiphenylsulfides, a series of dissymmetrical derivatives, corresponding to the replacement of one aromatic moiety by different amines, was synthesized. TR inhibition studies revealed the importance of the aromatic rings and of the amino groups in the side chains for potent inhibition. Quinonic moities were also introduced with the aim of acting as TR redox-cycling substrates.
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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 |
May
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pubmed:issn |
0960-894X
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
19
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pubmed:volume |
8
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1175-80
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:9871730-Animals,
pubmed-meshheading:9871730-Drug Design,
pubmed-meshheading:9871730-Enzyme Inhibitors,
pubmed-meshheading:9871730-Indicators and Reagents,
pubmed-meshheading:9871730-Kinetics,
pubmed-meshheading:9871730-Molecular Structure,
pubmed-meshheading:9871730-NADH, NADPH Oxidoreductases,
pubmed-meshheading:9871730-Structure-Activity Relationship,
pubmed-meshheading:9871730-Trypanocidal Agents,
pubmed-meshheading:9871730-Trypanosoma cruzi
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pubmed:year |
1998
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pubmed:articleTitle |
Structure-activity relationships in 2-aminodiphenylsulfides against trypanothione reductase from Trypanosoma cruzi.
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pubmed:affiliation |
Institut de Biologie, URA CNRS 1309, Faculté de Pharmacie, Lille, France.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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