Source:http://linkedlifedata.com/resource/pubmed/id/21549595
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
11
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pubmed:dateCreated |
2011-5-20
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pubmed:abstractText |
CEs are important enzymes that catalyze the hydrolysis of prodrugs. In this Letter, we present a new mechanistic ER-specific fluorescent probe 1 based on CE activity. Permeation of 1 into cells and subsequent hydrolytic activation by CEs causes spontaneously quinone methide cleavage, resulting in bright red fluorescence in ER with high specificity. Probe 1 was developed for CE activity imaging and inhibitor screening at the cellular level.
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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 |
Jun
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pubmed:issn |
1464-3405
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pubmed:author | |
pubmed:copyrightInfo |
Copyright © 2011 Elsevier Ltd. All rights reserved.
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pubmed:issnType |
Electronic
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pubmed:day |
1
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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 |
3206-9
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pubmed:meshHeading |
pubmed-meshheading:21549595-Animals,
pubmed-meshheading:21549595-COS Cells,
pubmed-meshheading:21549595-Carboxylesterase,
pubmed-meshheading:21549595-Cercopithecus aethiops,
pubmed-meshheading:21549595-Drug Design,
pubmed-meshheading:21549595-Endoplasmic Reticulum,
pubmed-meshheading:21549595-Fluorescent Dyes,
pubmed-meshheading:21549595-Indolequinones,
pubmed-meshheading:21549595-Molecular Structure
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pubmed:year |
2011
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pubmed:articleTitle |
Design and synthesis of an ER-specific fluorescent probe based on carboxylesterase activity with quinone methide cleavage process.
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pubmed:affiliation |
Department of Chemistry and Life Sciences, College of Bioresource Sciences, Nihon University, 1866 Kameino, Fujisawa-shi, Kanagawa 252-0880, Japan. hakamata.wataru@nihon-u.ac.jp
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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