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Discovery of Dehydrogenated Imipridone Derivatives as Activators of Human Caseinolytic Protease P
Journal of Medicinal ChemistryBased 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 +9 more
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Journal of the American Chemical Society, 2015
Caseinolytic protease P (ClpP) represents a central bacterial degradation machinery that is involved in cell homeostasis and pathogenicity. The functional role of ClpP has been studied by genetic knockouts and through the use of beta-lactones, which remain the only specific inhibitors of ClpP discovered to date.
Mathias W. Hackl +11 more
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Caseinolytic protease P (ClpP) represents a central bacterial degradation machinery that is involved in cell homeostasis and pathogenicity. The functional role of ClpP has been studied by genetic knockouts and through the use of beta-lactones, which remain the only specific inhibitors of ClpP discovered to date.
Mathias W. Hackl +11 more
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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 +6 more
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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 +6 more
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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 +4 more
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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 +4 more
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Inquiries into the Mycobacterial Caseinolytic Protease System
A thesis presented to the faculty of The Rockefeller University in partial fulfillment of the requirements for the degree of Doctor of ...openaire +1 more source
European Journal of Medicinal Chemistry
The caseinolytic protease (Clp) complex plays a fundamental role in protein homeostasis, ensuring the degradation of misfolded and damaged proteins in prokaryotic cells and eukaryotic organelles. Given its essential function, Clp has emerged as an attractive therapeutic target for bacterial infections, particularly for Mycobacterium tuberculosis (Mtb).
Andressa Franciélli Bonjorno +4 more
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The caseinolytic protease (Clp) complex plays a fundamental role in protein homeostasis, ensuring the degradation of misfolded and damaged proteins in prokaryotic cells and eukaryotic organelles. Given its essential function, Clp has emerged as an attractive therapeutic target for bacterial infections, particularly for Mycobacterium tuberculosis (Mtb).
Andressa Franciélli Bonjorno +4 more
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The Mechanism of Caseinolytic Protease (ClpP) Inhibition
Angewandte Chemie International Edition, 2013Malte Gersch +9 more
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Process Biochemistry
The caseinolytic protease (ClpP)-producing strain CHFM, isolated from Algerian goat milk, was identified as Lactiplantibacillus pentosus through 16 S rRNA sequence analysis. The optimal conditions for ClpP expression by Lpb. pentosus CHFM were determined in a modified MRS medium, where peptone was replaced with casein.
Zater, Zohra Yasmine +5 more
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The caseinolytic protease (ClpP)-producing strain CHFM, isolated from Algerian goat milk, was identified as Lactiplantibacillus pentosus through 16 S rRNA sequence analysis. The optimal conditions for ClpP expression by Lpb. pentosus CHFM were determined in a modified MRS medium, where peptone was replaced with casein.
Zater, Zohra Yasmine +5 more
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Journal of Medicinal Chemistry
Based on D9, a previously reported small-molecule agonist of hClpP, a class of novel hClpP activators with a pyrazololactam scaffold was designed and synthesized. Detailed structure-activity relationship studies (SAR) for this class of compounds led to the identification of compound 24, which potently activated recombinant hClpP in a proteolysis assay ...
Rui Tang +10 more
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Based on D9, a previously reported small-molecule agonist of hClpP, a class of novel hClpP activators with a pyrazololactam scaffold was designed and synthesized. Detailed structure-activity relationship studies (SAR) for this class of compounds led to the identification of compound 24, which potently activated recombinant hClpP in a proteolysis assay ...
Rui Tang +10 more
openaire +2 more sources