PMID-sentid	Pub_year	Sent_text	comp_official_name	comp_offset	protein_name	organism	prot_offset
34474040-0	2021	Myricetin protects mice against MRSA-related lethal pneumonia by targeting ClpP.	myricetin	0-9	caseinolytic mitochondrial matrix peptidase proteolytic subunit	Mus musculus	75-79
20437156-2	2010	The clpP mutation in a murine infection model has demonstrated both attenuation of virulence and a sensitivity to hydrogen peroxide.	Hydrogen Peroxide	114-131	caseinolytic mitochondrial matrix peptidase proteolytic subunit	Mus musculus	4-8
20437156-4	2010	Because macrophages play a major role in immune response and activated macrophages can kill microbes via oxygen-dependant mechanisms, we investigated the effect of the clpP mutation on its sensitivity to macrophage-mediated oxygen-dependant mechanisms.	Oxygen	224-230	caseinolytic mitochondrial matrix peptidase proteolytic subunit	Mus musculus	168-172
20437156-5	2010	The clpP mutant derived from D39 (serotype 2) exhibited a higher sensitivity to oxidative stresses such as reactive oxygen intermediates, reactive nitrogen intermediates, and H(2)O(2), but no sensitivity to osmotic stress (NaCl) and pH.	reactive oxygen	107-122	caseinolytic mitochondrial matrix peptidase proteolytic subunit	Mus musculus	4-8
20437156-5	2010	The clpP mutant derived from D39 (serotype 2) exhibited a higher sensitivity to oxidative stresses such as reactive oxygen intermediates, reactive nitrogen intermediates, and H(2)O(2), but no sensitivity to osmotic stress (NaCl) and pH.	Nitrogen	147-155	caseinolytic mitochondrial matrix peptidase proteolytic subunit	Mus musculus	4-8
20437156-6	2010	Moreover, viability of the clpP mutant was significantly increased in murine macrophage cells by treatment with S-methylisothiourea sulfate, which inhibits inducible nitric oxide synthase (iNOS) activity and subsequently elicits lower level secretions of nitric oxide (NO).	S-methylisothiopseudouronium	112-139	caseinolytic mitochondrial matrix peptidase proteolytic subunit	Mus musculus	27-31
20437156-6	2010	Moreover, viability of the clpP mutant was significantly increased in murine macrophage cells by treatment with S-methylisothiourea sulfate, which inhibits inducible nitric oxide synthase (iNOS) activity and subsequently elicits lower level secretions of nitric oxide (NO).	Nitric Oxide	166-178	caseinolytic mitochondrial matrix peptidase proteolytic subunit	Mus musculus	27-31
34474040-7	2021	We revealed that myricetin could effectively block the activity of ClpP without disturbing the growth of the bacteria and the Gln-47 and Met-31 residues were necessary for myricetin binding to ClpP.	myricetin	172-181	caseinolytic mitochondrial matrix peptidase proteolytic subunit	Mus musculus	67-71
34474040-7	2021	We revealed that myricetin could effectively block the activity of ClpP without disturbing the growth of the bacteria and the Gln-47 and Met-31 residues were necessary for myricetin binding to ClpP.	myricetin	172-181	caseinolytic mitochondrial matrix peptidase proteolytic subunit	Mus musculus	193-197
34474040-2	2021	A conserved serine protease, caseinolytic peptidase P (ClpP) in Staphylococcus aureus is highly associated with pathogenicity and has been claimed to be a novel antimicrobial target.	Serine	12-18	caseinolytic mitochondrial matrix peptidase proteolytic subunit	Mus musculus	55-59
34474040-5	2021	The binding of myricetin to ClpP was determined and the mechanism of action was elucidated by thermal shift assay, surface plasmon resonance, and molecular dynamics simulations.	myricetin	15-24	caseinolytic mitochondrial matrix peptidase proteolytic subunit	Mus musculus	28-32
34474040-7	2021	We revealed that myricetin could effectively block the activity of ClpP without disturbing the growth of the bacteria and the Gln-47 and Met-31 residues were necessary for myricetin binding to ClpP.	myricetin	17-26	caseinolytic mitochondrial matrix peptidase proteolytic subunit	Mus musculus	67-71
34474040-7	2021	We revealed that myricetin could effectively block the activity of ClpP without disturbing the growth of the bacteria and the Gln-47 and Met-31 residues were necessary for myricetin binding to ClpP.	myricetin	17-26	caseinolytic mitochondrial matrix peptidase proteolytic subunit	Mus musculus	193-197
34474040-7	2021	We revealed that myricetin could effectively block the activity of ClpP without disturbing the growth of the bacteria and the Gln-47 and Met-31 residues were necessary for myricetin binding to ClpP.	Glutamine	126-129	caseinolytic mitochondrial matrix peptidase proteolytic subunit	Mus musculus	67-71
34474040-7	2021	We revealed that myricetin could effectively block the activity of ClpP without disturbing the growth of the bacteria and the Gln-47 and Met-31 residues were necessary for myricetin binding to ClpP.	Glutamine	126-129	caseinolytic mitochondrial matrix peptidase proteolytic subunit	Mus musculus	193-197
33731338-1	2021	Caseinolytic mitochondrial matrix peptidase proteolytic subunit (CLPP) is a serine protease that degrades damaged or misfolded mitochondrial proteins.	Serine	76-82	caseinolytic mitochondrial matrix peptidase proteolytic subunit	Mus musculus	0-63
6647573-6	1983	Electrophoresis of solubilized McCoy cell lysate pellet revealed a 14C-polyamine conjugated protein peak with Mr approximately or equal to 70,000 (CLPP).	14c-polyamine	67-80	caseinolytic mitochondrial matrix peptidase proteolytic subunit	Mus musculus	147-151
6647573-7	1983	Both CLSP and CLPP contained bound polyamine.	Polyamines	35-44	caseinolytic mitochondrial matrix peptidase proteolytic subunit	Mus musculus	14-18
6647573-8	1983	The major CLSP polyamine was spermidine while spermine exceeded the other two polyamines (putrescine and spermidine) in CLPP.	Spermine	46-54	caseinolytic mitochondrial matrix peptidase proteolytic subunit	Mus musculus	120-124
6647573-8	1983	The major CLSP polyamine was spermidine while spermine exceeded the other two polyamines (putrescine and spermidine) in CLPP.	Polyamines	78-88	caseinolytic mitochondrial matrix peptidase proteolytic subunit	Mus musculus	120-124
6647573-8	1983	The major CLSP polyamine was spermidine while spermine exceeded the other two polyamines (putrescine and spermidine) in CLPP.	Putrescine	90-100	caseinolytic mitochondrial matrix peptidase proteolytic subunit	Mus musculus	120-124
6647573-8	1983	The major CLSP polyamine was spermidine while spermine exceeded the other two polyamines (putrescine and spermidine) in CLPP.	Spermidine	105-115	caseinolytic mitochondrial matrix peptidase proteolytic subunit	Mus musculus	120-124
6647573-9	1983	About 25% of the polyamines associated with CLSP and CLPP were covalently bound with the exception of CLSP putrescine where 62.1% was covalently bound.	Polyamines	17-27	caseinolytic mitochondrial matrix peptidase proteolytic subunit	Mus musculus	53-57
33731338-1	2021	Caseinolytic mitochondrial matrix peptidase proteolytic subunit (CLPP) is a serine protease that degrades damaged or misfolded mitochondrial proteins.	Serine	76-82	caseinolytic mitochondrial matrix peptidase proteolytic subunit	Mus musculus	65-69
33731338-5	2021	Depletion of the cyclic GMP-AMP (cGAS)-stimulator of IFN genes (STING) DNA sensing pathway reduces steady-state IFN-I signaling and abrogates the broad antiviral phenotype of CLPP-null cells.	cyclic guanosine monophosphate-adenosine monophosphate	17-31	caseinolytic mitochondrial matrix peptidase proteolytic subunit	Mus musculus	175-179
31304066-5	2019	High glucose and high fat can promote the mRNA and protein expression of CLPP in mitochondria.	Glucose	5-12	caseinolytic mitochondrial matrix peptidase proteolytic subunit	Mus musculus	73-77
31885916-5	2019	In the second experimental study, the effect of the beta-blocker esmolol was examined in CLP-P (group CLP-PE vs. CLP-P; n = 5 in each group).	esmolol	65-72	caseinolytic mitochondrial matrix peptidase proteolytic subunit	Mus musculus	89-94
30446247-10	2018	RESULT(S): In Clpp-knockout oocytes compared with WT, FAD tau1 and tau2 were longer and I was higher, NADH tau2 was longer, and F was lower.	NAD	102-106	caseinolytic mitochondrial matrix peptidase proteolytic subunit	Mus musculus	14-18
27208630-7	2016	The enhanced cell survival in response to paraquat or tert-Butyl hydroperoxide in Surf1(-/-) fibroblasts compared to wild-type fibroblasts is associated with induced expression of Lon, ClpP, and Hsp60, increased maximal respiration, and increased reserve capacity as measured using the Seahorse Extracellular Flux Analyzer.	Paraquat	42-50	caseinolytic mitochondrial matrix peptidase proteolytic subunit	Mus musculus	185-189
27208630-7	2016	The enhanced cell survival in response to paraquat or tert-Butyl hydroperoxide in Surf1(-/-) fibroblasts compared to wild-type fibroblasts is associated with induced expression of Lon, ClpP, and Hsp60, increased maximal respiration, and increased reserve capacity as measured using the Seahorse Extracellular Flux Analyzer.	tert-Butylhydroperoxide	54-78	caseinolytic mitochondrial matrix peptidase proteolytic subunit	Mus musculus	185-189
26721594-5	2016	Reduction of ClpP levels by ~70% in C2C12 muscle cells resulted in a number of mitochondrial alterations including reduced mitochondrial respiration and reduced oxygen consumption rate in response to electron transport chain (ETC) complex I and II substrates.	Oxygen	161-167	caseinolytic mitochondrial matrix peptidase proteolytic subunit	Mus musculus	13-17
26721594-7	2016	In addition, ClpP deficient cells showed increased generation of reactive oxygen species (ROS) and decreased membrane potential.	Reactive Oxygen Species	65-88	caseinolytic mitochondrial matrix peptidase proteolytic subunit	Mus musculus	13-17
26721594-7	2016	In addition, ClpP deficient cells showed increased generation of reactive oxygen species (ROS) and decreased membrane potential.	Reactive Oxygen Species	90-93	caseinolytic mitochondrial matrix peptidase proteolytic subunit	Mus musculus	13-17