Abstract
Several compounds designed as bisubstrate analogues of protein farnesyltransferase inhibited the prenyl protein-specific protease Rce1, qualifying them as lead structures for a novel class of non-peptidic, non-prenylic inhibitors of this protease.
Publication types
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Alkyl and Aryl Transferases / antagonists & inhibitors
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Combinatorial Chemistry Techniques
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Endopeptidases / drug effects*
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Farnesyltranstransferase
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Humans
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Inhibitory Concentration 50
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Molecular Mimicry
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Peptides / chemical synthesis
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Peptides / pharmacology
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Protease Inhibitors / chemical synthesis*
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Protease Inhibitors / pharmacology
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Structure-Activity Relationship
Substances
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Peptides
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Protease Inhibitors
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Alkyl and Aryl Transferases
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Farnesyltranstransferase
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Endopeptidases
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RCE1 protein, human