Source:http://linkedlifedata.com/resource/pubmed/id/20691510
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
10
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pubmed:dateCreated |
2010-8-30
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pubmed:abstractText |
Six transition metal compounds of Schiff base ligands were evaluated for the inhibitory activity on jack bean urease, of which compounds 2-6 were determined by single crystal X-ray analysis. It was found that copper(II) complexes 1 and 4 showed strong inhibitory activity against jack bean urease (IC(50) = 0.52 and 0.46 microM), compared with acetohydroxamic acid (IC(50) = 42.12 microM) as a positive reference. Cobalt(II), nickel(II) and zinc(II) compounds also exhibited potent inhibitory activity (IC(50) = 3.88-25.20 microM). A docking analysis using the AUTODOCK 4.0 program could explain the inhibitory activities of 1 and 4 against urease.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Coordination Complexes,
http://linkedlifedata.com/resource/pubmed/chemical/Enzyme Inhibitors,
http://linkedlifedata.com/resource/pubmed/chemical/Schiff Bases,
http://linkedlifedata.com/resource/pubmed/chemical/Transition Elements,
http://linkedlifedata.com/resource/pubmed/chemical/Urease
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pubmed:status |
MEDLINE
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pubmed:month |
Oct
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pubmed:issn |
1768-3254
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pubmed:author | |
pubmed:copyrightInfo |
Copyright (c) 2010 Elsevier Masson SAS. All rights reserved.
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pubmed:issnType |
Electronic
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pubmed:volume |
45
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
4473-8
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pubmed:meshHeading |
pubmed-meshheading:20691510-Canavalia,
pubmed-meshheading:20691510-Coordination Complexes,
pubmed-meshheading:20691510-Crystallography, X-Ray,
pubmed-meshheading:20691510-Enzyme Inhibitors,
pubmed-meshheading:20691510-Models, Molecular,
pubmed-meshheading:20691510-Protein Binding,
pubmed-meshheading:20691510-Schiff Bases,
pubmed-meshheading:20691510-Transition Elements,
pubmed-meshheading:20691510-Urease
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pubmed:year |
2010
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pubmed:articleTitle |
Synthesis, molecular docking and biological evaluation of Schiff base transition metal complexes as potential urease inhibitors.
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pubmed:affiliation |
Engineering Research Center for Clean Production of Textile Printing, Ministry of Education, Wuhan Textile University, Wuhan 430073, People's Republic of China.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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