Abstract
We report comprehensive structure-activity relationship studies on a novel series of c-Jun N-terminal kinase (JNK) inhibitors. Intriguingly, the compounds have a dual inhibitory activity by functioning as both ATP and JIP mimetics, possibly by binding to both the ATP binding site and to the docking site of the kinase. Several of such novel compounds display potent JNK inhibitory profiles both in vitro and in cell.
Copyright © 2011 Elsevier Ltd. All rights reserved.
Publication types
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Research Support, N.I.H., Extramural
MeSH terms
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Adenosine Triphosphate
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Binding Sites
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Cell Line
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Drug Design
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Humans
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JNK Mitogen-Activated Protein Kinases / antagonists & inhibitors*
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Molecular Mimicry
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Protein Binding
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Protein Kinase Inhibitors / chemical synthesis*
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Protein Kinase Inhibitors / pharmacology
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Structure-Activity Relationship
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Thiophenes / chemistry
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Thiophenes / pharmacology*
Substances
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Protein Kinase Inhibitors
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Thiophenes
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thiophene-3-carboxylic acid
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Adenosine Triphosphate
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JNK Mitogen-Activated Protein Kinases