Results 161 to 170 of about 4,588 (199)

Targeting caseinolytic protease P and its AAA1 chaperone for tuberculosis treatment

Drug Discovery Today, 2023
Caseinolytic protease P with its AAA1 chaperone, known as Mycobacterium tuberculosis (Mtb)ClpP1P2 proteolytic machinery, maintains protein homeostasis in Mtb cells and is essential for bacterial survival. It is regarded as an important biological target with the potential to address the increasingly serious issue of multidrug-resistant (MDR) TB.
Xin, Xu, Laiying, Zhang, Tao, Yang, Zhiqiang, Qiu, Lang, Bai, Youfu, Luo   +5 more
openaire   +2 more sources

Identification, structure, and caseinolytic properties of milk-clotting proteases from Moringa oleifera flowers

Food Research International, 2022
The protein extract of Moringa oleifera flowers is reported to have milk-clotting activity (MCA), but information regarding its protease is unclear. In this study, two milk-clotting proteases (MoFP 12 and MoFP 13) with molecular weights of 42.304 kDa and 31.741 kDa, respectively, were isolated and identified from M.
Qiong, Zhao, Aixiang, Huang, Gaizhuan, Wu, Qian, Guo, Mei, Li, Xuefeng, Wang   +5 more
openaire   +2 more sources

Selective Activation of Human Caseinolytic Protease P (ClpP)

Angewandte Chemie International Edition, 2018
AbstractCaseinolytic protease P (ClpP) is the proteolytic component of the ClpXP protein degradation complex. Eukaryotic ClpP was recently found to act within the mitochondria‐specific unfolded protein response (UPRmt). However, its detailed function and dedicated regulation remain largely unexplored.
Matthias Stahl, Vadim S. Korotkov, Dóra Balogh, Leonhard M. Kick, Malte Gersch, Axel Pahl, Pavel Kielkowski, Klaus Richter, Sabine Schneider, Stephan A. Sieber   +9 more
openaire   +2 more sources

Design and synthesis of tailored human caseinolytic protease P inhibitors

Chemical Communications, 2018
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.
Thomas F. Gronauer, Melanie M. Mandl, Markus Lakemeyer, Mathias W. Hackl, Martina Meßner, Vadim S. Korotkov, Johanna Pachmayr, Stephan A. Sieber   +7 more
openaire   +2 more sources

Tamarixetin Attenuated the Virulence of Staphylococcus aureus by Directly Targeting Caseinolytic Protease P

Journal of Natural Products, 2022
Staphylococcus aureus, especially drug-resistant S. aureus infections, is a worldwide healthcare challenge. There is a growing focus on antivirulence therapy against S. aureus. Caseinolytic protease p (ClpP) is a protein hydrolase essential for pathogenicity in S. aureus.
Wu Song, Bingmei Wang, Liyan Sui, Yan Shi, Xinran Ren, Xingye Wang, Xiangri Kong, Juan Hou, Li Wang, Lin Wei, Yanhe Luan, Jiyu Guan, Yicheng Zhao   +12 more
openaire   +2 more sources

Antibodies against homologous microbial caseinolytic proteases P characterise primary biliary cirrhosis

Journal of Hepatology, 2002
Antibodies to caseinolytic protease P(177-194) (ClpP(177-194)) of the proteolytic subunit of the Clp complex of Escherichia coli (E. coli) are uniquely present in primary biliary cirrhosis (PBC). Molecular mimicry between the regulatory subunit ClpX and the principal T-cell epitope of pyruvate dehydrogenase complex (PDC-E2) in PBC, has been proposed to
Bogdanos, D P, Baum, H, Sharma, U C, Grasso, A, Ma, Y, Burroughs, A K, Vergani, D   +6 more
openaire   +3 more sources

31–27 kDa Caseinolytic Protease in Human Tears

1998
Normal wound healing requires the presence and regulation of cell adhesion proteins, proteases, and growth and other factors. Several of the proteases involved in tissue remodeling and wound healing have been detected in tear fluid. Previous studies on ocular pathologies have focused on the plasminogen-plasmin system1,2 and its role in fibrinolysis ...
M, Sakata, A R, Beaton, S, Sathe, R A, Sack   +3 more
openaire   +2 more sources

Structure and Mechanism of the Caseinolytic Protease ClpP1/2 Heterocomplex from Listeria monocytogenes

Angewandte Chemie International Edition, 2015
AbstractListeria monocytogenes is a devastating bacterial pathogen. Its virulence and intracellular stress tolerance are supported by caseinolytic protease P (ClpP), an enzyme that is conserved among bacteria. L. monocytogenes expresses two ClpP isoforms that are only distantly related by sequence and differ in catalysis, oligomerization, active‐site ...
Maria Dahmen, Marie-Theres Vielberg, Michael Groll, Stephan A. Sieber   +3 more
openaire   +2 more sources

Discovery of Dehydrogenated Imipridone Derivatives as Activators of Human Caseinolytic Protease P

Journal of Medicinal Chemistry
Based on the founding member of imipridones, ONC201, a class of dehydrogenated imipridone derivatives was designed, synthesized, and evaluated in a series of biochemical and biological assays as human caseinolytic protease P (hClpP) activators. Mechanism studies for one of the most potent compounds, XT6, indicated that it can potently bind to both ...
Jinxin Jiang, Guangjun Xie, Tong Li, Hao Ding, Rui Tang, Jiajun Luo, Qiannan Li, Wugang Lu, Yibei Xiao, Haiying Sun   +9 more
openaire   +2 more sources

Mutation analysis of the interactions between Mycobacterium tuberculosis caseinolytic protease C1 (ClpC1) and ecumicin

International Journal of Biological Macromolecules, 2017
Ecumicin is a well-known and potent inhibitor of Mycobacterium tuberculosis. Although the target of ecumicin is caseinolytic protease C1 (ClpC1), the exact mechanism by which ecumicin inhibits ClpC1 has not been identified. To analyze ecumicin's action on ClpC1, site-directed mutagenesis was performed on its binding site. The estimated binding residues
In-Pil, Jung, Na-Reum, Ha, A-Ru, Kim, Sang-Heon, Kim, Moon-Young, Yoon   +4 more
openaire   +2 more sources