ATP non-competitive Ser/Thr kinase inhibitors as potential anticancer agents.
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.
Dipartimento di Scienze Farmaceutiche, Università di Padova, Padova, Italy.
Giorgio
G
Cozza
Andrea
A
Bortolato
Ernesto
E
Menta
Ennio
E
Cavalletti
Silvano
S
Spinelli
Stefano
S
Moro
D000255:Adenosine Triphosphate / Q000378:metabolism*; D000970:Antineoplastic Agents / Q000494:pharmacology* / Q000627:therapeutic use; D006801:Humans; D008958:Models, Molecular; D010766:Phosphorylation / Q000187:drug effects; D011487:Protein Conformation; D047428:Protein Kinase Inhibitors / Q000494:pharmacology* / Q000627:therapeutic use; D017346:Protein Serine-Threonine Kinases / Q000037:antagonists & inhibitors* / Q000378:metabolism
D000970:Antineoplastic Agents; D047428:Protein Kinase Inhibitors; D000255:Adenosine Triphosphate; D017346:Protein Serine-Threonine Kinases