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Results 1 - 8 of 8
EC Number
Activating Compound
acyldepsipeptides in addition to opening the axial pore directly stimulate ClpP activity through cooperative binding
allow the protease to degrade folded native proteins in the absence of its cognate chaperones
ADEP series 2, 3, 4 as well as two other synthesized derivatives, IDR-10001 and IDR-10011, which incorporate N-methylalanine instead of the more rigid homoproline in the depsipeptide core structure. All five compound are active against Mycobacterium tuberculosis, ADEP2 is the most active
stimulates proteolytic activity of ClpP in heart mitochondria of muscle creatine kinase mutants
ClpX binding stimulates ClpP cleavage of peptides larger than a few amino acids and enhances ClpP active-site modification. Stimulation requires ATP binding but not hydrolysis by ClpX
carbonyl cyanide m-chloro phenylhydrazone and 2,4-dinitrophenol induce the heat-shock-like response, cellular level of the heat shock regulator protein sigma-32 also increases
ClpP3/R complex stimulates the steady-state ATPase activity of ClpC
frataxin deficiency causes significant upregulation of both mitochondrial Lon and ClpP proteases in the cardiac mouse model for Friedreich ataxia. ClpP protein level is progressively enhanced, with ca. 3fold, 3.5fold and 4.5fold increases at 5, 7 and 10 weeks of age in muscle creatine kinase mutants, respectively, despite no change in mRNA levels
Results 1 - 8 of 8