Abstract
The serine protease urokinase plasminogen activator (uPA) is thought to play a central role in tumor metastasis and angiogenesis. Molecular modeling studies suggest that 5-thiomethylthiopheneamidine inhibits uPA by binding at the S1 pocket of the active site. Further structure based elaboration of this residue resulted in a novel class of potent and selective inhibitors of uPA.
MeSH terms
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Antimetabolites / chemical synthesis
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Antimetabolites / chemistry
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Antimetabolites / pharmacology*
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Binding Sites
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Humans
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Structure-Activity Relationship
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Thiophenes / chemical synthesis
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Thiophenes / chemistry
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Thiophenes / pharmacology*
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Urokinase-Type Plasminogen Activator / antagonists & inhibitors*
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Urokinase-Type Plasminogen Activator / physiology
Substances
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Antimetabolites
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Thiophenes
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Urokinase-Type Plasminogen Activator