Source:http://linkedlifedata.com/resource/pubmed/id/19747823
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
20
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pubmed:dateCreated |
2009-9-28
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pubmed:abstractText |
A FRET peptide substrate was synthesized and evaluated for enzymatic cleavage by the BoNT/B light chain protease. The FRET substrate was found to be useful in both a high throughput assay to uncover initial 'hits' and a low throughput HPLC assay to determine kinetic parameters and modes of inhibition.
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pubmed:grant | |
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 |
Oct
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pubmed:issn |
1464-3405
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pubmed:author | |
pubmed:issnType |
Electronic
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pubmed:day |
15
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pubmed:volume |
19
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
5848-50
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pubmed:dateRevised |
2010-12-3
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pubmed:meshHeading |
pubmed-meshheading:19747823-Amino Acid Sequence,
pubmed-meshheading:19747823-Botulinum Toxins,
pubmed-meshheading:19747823-Fluorescence Resonance Energy Transfer,
pubmed-meshheading:19747823-Molecular Sequence Data,
pubmed-meshheading:19747823-Peptides,
pubmed-meshheading:19747823-Protease Inhibitors
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pubmed:year |
2009
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pubmed:articleTitle |
Synthetic substrate for application in both high and low throughput assays for botulinum neurotoxin B protease inhibitors.
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pubmed:affiliation |
Department of Chemistry and The Skaggs Institute for Chemical Biology, The Scripps Research Institute, La Jolla, CA 92037, USA.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't,
Research Support, N.I.H., Extramural
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