Abstract
Protein kinases are one of the largest known families of enzyme characterized by having a well conserved ATP binding pocket. Most of the synthetic kinase inhibitors are ATP-competitive, but display some potential problems, like selectivity, discrepancy between the in vitro and in vivo inhibition assays and an high risk of developing mutation inside the ATP-binding pocket. Recently some new inhibitors with a non-competitive mechanism of action were reported, with interesting results both in vitro and in vivo.
Publication types
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Research Support, Non-U.S. Gov't
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Review
MeSH terms
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Adenosine Triphosphate / metabolism*
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Antineoplastic Agents / pharmacology*
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Antineoplastic Agents / therapeutic use
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Humans
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Models, Molecular
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Phosphorylation / drug effects
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Protein Conformation
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Protein Kinase Inhibitors / pharmacology*
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Protein Kinase Inhibitors / therapeutic use
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Protein Serine-Threonine Kinases / antagonists & inhibitors*
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Protein Serine-Threonine Kinases / metabolism
Substances
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Antineoplastic Agents
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Protein Kinase Inhibitors
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Adenosine Triphosphate
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Protein Serine-Threonine Kinases