TY  -  
T1  - Identification and characterization of approved drugs and drug-like compounds as covalent Escherichia coli ClpP inhibitors 
SN  -  /  
UR  - http://hdl.handle.net/10138/304244 
T3  -  
A1  - Sassetti, Elisa; Cruz, Cristina Durante; Tammela, Päivi; Winterhalter, Mathias; Augustyns, Koen; Gribbon, Philip; Windshügel, Björn 
A2  -  
PB  -  
Y1  - 2019 
LA  - eng 
AB  - The serine protease Caseinolytic protease subunit P (ClpP) plays an important role for protein homeostasis in bacteria and contributes to various developmental processes, as well as virulence. Therefore, ClpP is considered as a potential drug target in Gram-positive and Gram-negative bacteria. In this study, we utilized a biochemical assay to screen several small molecule libraries of approved and investigational drugs for Escherichia coli ClpP inhibitors. The approved drugs bortezomib, cefmetaz... 
VO  -  
IS  -  
SP  -  
OP  -  
KW  - ACID; ANTIBIOTIC-RESISTANCE; ClpP; Escherichia coli; FAMILY; PROTEASE; RECOGNITION; covalent binding; high-throughput screening; inhibitor; nitric oxide stress; surface plasmon resonance; 317 Pharmacy; 1182 Biochemistry, cell and molecular biology; 116 Chemical sciences 
N1  -   
PP  -  
ER  -