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ProteomicsAblation of mitochondrial rhomboid Parl causes Leigh syndrome
The mitochondrial intramembrane rhomboid protease Parl plays essential roles in cell death but its physiological contribution remains unclear. In the present study we show that Parl ablation causes a dramatic necrotic neurodegeneration consistent with Leigh syndrome, a mitochondrial disease characte...
ORGANISM(S): Mus musculus (Mouse) 
2018-11-21 | PXD008908 | Pride
Leigh syndrome Pgam5 Rhomboids Proteolysis Necrosis Ttc19 Complex iii Apoptosis Neurodegeneration Parl Pink1 
ProteomicsThe rhomboid protease PARL regulates apoptosis via proteolytic maturation of Smac/DIABLO in mitochondria
Substrates of the mitochondrial protease PARL were identified using quantitative N-terminal ChaFRADIC:
ORGANISM(S): Homo sapiens (Human) 
2017-03-09 | PXD005535 | Pride
Parl substrates Chafradic N-terminomics 
UnknownInsights into the catalytic properties of the mitochondrial rhomboid protease PARL.
Not available
S-EPMC7966987 | biostudies-literature
UnknownPARL deficiency in mouse causes Complex III defects, coenzyme Q depletion, and Leigh-like syndrome.
Not available
S-EPMC6320509 | biostudies-literature
UnknownMitochondrial defects caused by PARL deficiency lead to arrested spermatogenesis and ferroptosis.
Not available
S-EPMC10519710 | biostudies-literature
ProteomicsMultiplex Substrate Profiling of the human mitochondrial rhomboid protease PARL by mass spectrometry
The mammalian mitochondrial rhomboid protease PARL is a critical regulator of mitochondrial homeostasis through its cleavage of substrates such as PINK1, PGAM5, and Smac, which have roles in mitochondrial quality control and apoptosis. Here are the LC-MS/MS data of Multiplex substrate profiling resu...
ORGANISM(S): Synthetic Construct (ncbitaxon:32630) 
2020-04-16 | MSV000085295 | MassIVE
ProteomicsCLPB disaggregase dysfunction impacts the functional integrity of the proteolytic SPY complex
CLPB is a mitochondrial intermembrane space AAA+ domain–containing disaggregase. CLPB mutations are associated with 3-methylglutaconic aciduria and neutropenia; however, the molecular mechanism underscoring disease and the contribution of CLPB substrates to disease pathology remains unknown. Interac...
ORGANISM(S): Homo sapiens (Human) 
2024-01-18 | PXD042313 | Pride
Disaggregase Protein transport Mitochondria Protein quality control Mitochondrial disease 
UnknownCLPB disaggregase dysfunction impacts the functional integrity of the proteolytic SPY complex.
Not available
S-EPMC10818064 | biostudies-literature
UnknownSubstrate recognition by the human mitochondrial processing peptidase and its processing of PINK1.
Not available
S-EPMC12670562 | biostudies-literature
UnknownOMA1-An integral membrane protease?
Not available
S-EPMC7770061 | biostudies-literature
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