Design and synthesis of tailored human caseinolytic protease P inhibitors
Copyright policy )Design and synthesis of tailored human caseinolytic protease P inhibitors
To expedite functional studies of human ClpP we introduce tailored small molecule inhibitors. These compounds are active against the proteolytic ClpXP complex. Target identification elucidates anti-proliferative effects against cancer cells.
Staphylococcus aureus, Escherichia coli Proteins, Antineoplastic Agents, Apoptosis, Endopeptidase Clp, Structure-Activity Relationship, Cell Movement, Cell Line, Tumor, Drug Design, Escherichia coli, ATPases Associated with Diverse Cellular Activities, Humans, Kallikreins, Protease Inhibitors, Benzofurans, Molecular Chaperones
Staphylococcus aureus, Escherichia coli Proteins, Antineoplastic Agents, Apoptosis, Endopeptidase Clp, Structure-Activity Relationship, Cell Movement, Cell Line, Tumor, Drug Design, Escherichia coli, ATPases Associated with Diverse Cellular Activities, Humans, Kallikreins, Protease Inhibitors, Benzofurans, Molecular Chaperones
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