Results 141 to 150 of about 147,909 (161)
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31–27 kDa Caseinolytic Protease in Human Tears
1998Normal 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 +3 more
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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 +12 more
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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 +12 more
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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 +3 more
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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 +3 more
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Caseinolytic Protease P: A Therapeutic Nexus in Infection, Inflammation, and Immunity
Critical Reviews in ImmunologyCaseinolytic protease P (ClpP) is a highly conserved serine protease that plays a pivotal role in protein homeostasis and quality control in bacteria, mitochondria of mammalian cells, and plant chloroplasts. As the proteolytic core of the ATP-dependent Clp protease complex, ClpP partners with regulatory ATPases (e.g., ClpX, ClpA) to degrade misfolded ...
Shreya S, Sonak +3 more
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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).
Jean Leandro Dos Santos +2 more
exaly +3 more sources
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).
Jean Leandro Dos Santos +2 more
exaly +3 more sources
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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Discovery of Activators of Human Caseinolytic Protease P with a Benzolactam Scaffold
Journal of Medicinal ChemistryBased on compound 1, a previously identified activator of human caseinolytic protease P (hClpP) containing a pyrazololactam scaffold, a class of benzolactam derivatives was designed through a scaffold-hopping strategy. Structural optimization of this series led to the identification of LZL25, which potently activated recombinant hClpP with an EC50 of 0.
Zhilong Li +8 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