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ProteomicsDesign and synthesis of tailored human caseinolytic protease P inhibitors
Human caseinolytic protease P (hClpP) is important for degradation of misfolded proteins in the mitochondrial unfolded protein response. We here introduce tailored hClpP inhibitors that utilize a steric discrimination in their core naphthofuran scaffold to selectively address the human enzyme. This ...
ORGANISM(S): Homo sapiens (Human) 
2019-03-05 | PXD010277 | Pride
Mitochondria Jurkat Clpp Huh7 Phenyl esters 
ProteomicsA Photocrosslinking Probe to Capture the Substrates of Caseinolytic Protease P
Protein homeostasis in bacteria is regulated by proteases such as the tetradecameric caseinolytic protease P (ClpP). Although substrates of ClpP have been successfully deciphered in genetically engineered cells, methods which directly trap processed proteins within native cells remain elusive. Here,...
ORGANISM(S): Staphylococcus aureus 
2024-10-04 | PXD047274 | Pride
S. aureus Substrates 
UnknownPlastid caseinolytic protease OsClpR1 regulates chloroplast development and chloroplast RNA editing in rice.
Not available
S-EPMC8137786 | biostudies-literature
ProteomicsSubstrate profiling of mitochondrial caseinolytic protease P via a site-specific photocrosslinking approach
The function of proteases is mainly determined by the substrates they are processing. However, substrate identification remains a challenging task. Here, we used genetic code expansion to incorporate a diazirine-lysine amino acid (DiazK) at selected positions of mitochondrial caseinolytic protease P...
ORGANISM(S): Homo sapiens (Human) 
2023-08-22 | PXD027954 | Pride
Mtupr Mitochondria Photoaffinity crosslinking Clpxp Orbitrap fusion 
UnknownThe structure of caseinolytic protease subunit ClpP2 reveals a functional model of the caseinolytic protease system from Chlamydia trachomatis.
Not available
S-EPMC9823225 | biostudies-literature
ProteomicsAcyldepsipeptide probes facilitate specific detection of caseinolytic protease P independent of its oligomeric and activity state
Caseinolytic protease P (ClpP) is a tetradecameric peptidase which assembles with chaperones such as ClpX to gain proteolytic activity. Acyldepsipeptides (ADEPs) represent small molecule mimics of ClpX, which bind into hydrophobic pockets on the apical site of the complex and thereby induce activati...
ORGANISM(S): Staphylococcus aureus 
2020-05-26 | PXD015244 | Pride
Thermo fischer q exactive orbitrap Photoaffinity labeling S. aureus 
UnknownCaseinolytic mitochondrial matrix peptidase X is essential for homologous chromosome synapsis and recombination during meiosis of male mouse germ cells.
Not available
S-EPMC10919424 | biostudies-literature
UnknownStructure-guided development of selective caseinolytic protease P agonists as antistaphylococcal agents.
Not available
S-EPMC11722091 | biostudies-literature
ProteomicsAnt yogurt LC-MS caseinolytic potential
Our hypothesis was that the ant holobiont may contribute enzymes, in particular proteases, that modify the yogurt texture. To test this hypothesis, we conducted an untargeted proteomics analysis based on a self-curated database that contained proteases from Formica ants, ant-yogurt bacteria, convent...
ORGANISM(S): Bos taurus (Bovine) Fructilactobacillus sanfranciscensis DSM 20451 Oecophyllibacter saccharovorans Streptococcus thermophilus MTCC 5460 Lactobacillus delbrueckii subsp. bulgaricus CNCM I-1632 Formica sp. BOLD:AAA1469 Wolbachia endosymbiont of Schlechtendalia chinensis 
2025-08-01 | PXD057843 | Pride
Caseinolytic Ant Yogurt 
UnknownReprogramming of the Caseinolytic Protease by ADEP Antibiotics: Molecular Mechanism, Cellular Consequences, Therapeutic Potential.
Not available
S-EPMC8182300 | biostudies-literature
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