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ProteomicsA quantitative proteomics screen identifies a substrate repertoire of rhomboid protease RHBDL2 in human cells and implicates it in epithelial homeostasis.
Rhomboids are intramembrane serine proteases conserved in all kingdoms of life. They regulate epidermal growth factor receptor signalling in Drosophila by releasing signalling ligands from their transmembrane tethers. Their functions in mammals are poorly understood, in part because of the lack of e...
ORGANISM(S): Homo sapiens (Human) 
2017-08-14 | PXD006716 | Pride
Proteomics Ectodomain shedding Intramembrane protease Epithelia Rhomboid protease Substrate 
ProteomicsSubstrate specificity of Pseudomonas aeruginosa protease LasB using multiplex substrate profiling by mass spectrometry
Substrate specificity of Pseudomonas aeruginosa protease LasB using multiplex substrate profiling by mass spectrometry
ORGANISM(S): Synthetic 228-peptide Library 
2017-08-18 | MSV000081465 | MassIVE
ProteomicsSubstrate specificity of Pseudomonas aeruginosa protease LasB using multiplex substrate profiling by mass spectrometry
Substrate specificity of Pseudomonas aeruginosa protease LasB using multiplex substrate profiling by mass spectrometry
ORGANISM(S): Pseudomonas Aeruginosa (ncbitaxon:287) 
2017-10-18 | MSV000081623 | MassIVE
ProteomicsStructural basis for the mechanisms of human presequence protease conformational switch and substrate recognition
Presequence protease (PreP) degrades presequence peptides cleaved off from nuclear-encoded proteins and other aggregation-prone peptides, such as amyloid β (Aβ). PreP structures have only been determined in a closed conformation; thus, the mechanisms of substrate binding and selectivity remain elusi...
ORGANISM(S): Homo sapiens (Human) 
2022-05-20 | PXD029542 | Pride
Amyloid peptide Hdxms Presequence protease Cryoem 
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 
ProteomicsTime-resolved inducible knock-down of Clp protease subunits in tobacco identifies putative protease substrates
The Clp protease complex in plants is the one with the highest complexity through all life kingdoms. It is composed of 14 nuclear- and plastid-encoded subunits which are allocated in different rings across the complex. The proteolytic ring (P-ring; ClpP3-ClpP6) and non-proteolytic ring (R-ring; ClpR...
ORGANISM(S): Arabidopsis thaliana (Mouse-ear cress) 
2022-02-22 | PXD008305 | Pride
Clp protease  chloroplast  protein degradation  protease substrate  nicotiana tabacum  inducible rnai  lc-msms  shotgun proteomics 
UnknownHIV-1 Protease and Substrate Coevolution Validates the Substrate Envelope As the Substrate Recognition Pattern.
Not available
S-EPMC3862175 | biostudies-literature
ProteomicsA chemical strategy for protease substrate profiling
Here, we introduce a simple method, termed CHOPS, for the discovery of protease substrates. CHOPS exploits a 2-pyridinecarboxaldehyde (2PCA)-biotin probe, which selectively biotinylates protein N-termini except those with proline in the second position. CHOPS can, in theory, discover substrates for...
ORGANISM(S): Homo sapiens (Human) 
2019-04-23 | PXD013019 | Pride
Chops Silac N-terminomics 
ProteomicsMPP profiling in yeast - Quantitative profiling for substrates of the mitochondrial presequence processing protease reveals a set of non-substrate proteins increased upon proteotoxic stress
The majority of mitochondrial preproteins is targeted via N-terminal presequences that are cleaved upon import into the organelle. The essential mitochondrial processing protease (MPP) is assumed to cleave the majority of incoming precursors. However, only few substrate proteins of MPP have been exp...
ORGANISM(S): Saccharomyces cerevisiae (Baker's yeast) 
2015-10-14 | PXD002063 | Pride
Mitochondrial processing protease mpp Mitochondria Chafradic Mitochondrial stress response Presequence import pathway 
UnknownHIV-1 protease-substrate coevolution in nelfinavir resistance.
Not available
S-EPMC4054462 | biostudies-literature
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