Source:http://linkedlifedata.com/resource/pubmed/id/18205296
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
3
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pubmed:dateCreated |
2008-2-8
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pubmed:abstractText |
The use of protein ESI mass spectrometry under non-denaturing conditions to analyze a dynamic combinatorial library of thiols/disulfides with the BcII metallo-beta-lactamase enabled the rapid identification of an inhibitor with a K(i) of < 1 microM. The study exemplifies the utility of protein-MS for screening dynamic mixtures of potential enzyme-inhibitors.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
Feb
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pubmed:issn |
0022-2623
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
14
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pubmed:volume |
51
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
684-8
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pubmed:meshHeading |
pubmed-meshheading:18205296-Kinetics,
pubmed-meshheading:18205296-Models, Molecular,
pubmed-meshheading:18205296-Spectrometry, Mass, Electrospray Ionization,
pubmed-meshheading:18205296-Structure-Activity Relationship,
pubmed-meshheading:18205296-Sulfhydryl Compounds,
pubmed-meshheading:18205296-beta-Lactamases
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pubmed:year |
2008
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pubmed:articleTitle |
Dynamic combinatorial mass spectrometry leads to metallo-beta-lactamase inhibitors.
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pubmed:affiliation |
Chemistry Research Laboratory and OCISB, Oxford, UK.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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