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rdf:type |
|
|
lifeskim:mentions |
|
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pubmed:issue |
19
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pubmed:dateCreated |
2010-9-13
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pubmed:abstractText |
Most human histamine H(3) receptor (hH(3)R) antagonists follow a general structural blueprint, containing a basic moiety linked by a spacer to a substituted core element. In this investigation the acceptance of thiazol-2-yl ether moieties in the core region is proved with some ether derivatives showing hH(3)R binding affinities in the nanomolar concentration range. A diversity of structural motifs is used as substituents to enhance the in vitro hH(3)R binding affinity.
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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 |
Oct
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pubmed:issn |
1464-3405
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pubmed:author |
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pubmed:copyrightInfo |
Copyright © 2010 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 |
20
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pubmed:owner |
NLM
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|
pubmed:authorsComplete |
Y
|
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pubmed:pagination |
5879-82
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pubmed:meshHeading |
|
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pubmed:year |
2010
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|
pubmed:articleTitle |
Azole derivatives as histamine H3 receptor antagonists, part I: thiazol-2-yl ethers.
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|
pubmed:affiliation |
Johann Wolfgang Goethe University, Institute of Pharmaceutical Chemistry, Biocenter, ZAFES/LiFF/CMP/ICNF, Max-von-Laue-Str 9, 60438 Frankfurt, Germany.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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