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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
8
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pubmed:dateCreated |
2011-4-4
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pubmed:abstractText |
Leucine aminopeptidases (LAPs) are widely distributed in organisms from bacteria to humans, and play crucial roles in cell maintenance and cell growth. Thus, assays for LAP are necessary for measuring its activity and inhibitor potency. In this Letter, we report a small-molecule probe which exhibits colorimetric and fluorogenic changes according to LAP activity.
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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 |
Apr
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pubmed:issn |
1464-3405
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pubmed:author |
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pubmed:copyrightInfo |
Copyright © 2011 Elsevier Ltd. All rights reserved.
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pubmed:issnType |
Electronic
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pubmed:day |
15
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pubmed:volume |
21
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
2403-5
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pubmed:meshHeading |
pubmed-meshheading:21396812-Calorimetry,
pubmed-meshheading:21396812-Cell Line, Tumor,
pubmed-meshheading:21396812-Fluorescent Dyes,
pubmed-meshheading:21396812-Furans,
pubmed-meshheading:21396812-Humans,
pubmed-meshheading:21396812-Kinetics,
pubmed-meshheading:21396812-Leucyl Aminopeptidase,
pubmed-meshheading:21396812-Nitriles,
pubmed-meshheading:21396812-Protease Inhibitors,
pubmed-meshheading:21396812-Small Molecule Libraries
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pubmed:year |
2011
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|
pubmed:articleTitle |
Small-molecule probe using dual signals to monitor leucine aminopeptidase activity.
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pubmed:affiliation |
Department of Chemistry, College of Natural Sciences, Seoul National University, Seoul 151-747, Republic of Korea.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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