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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 
ProteomicsToxoplasma gondii aspartyl protease 3
The micronemes and rhoptries are specialized organelles that secrete their contents at the apical tip of apicomplexan parasites in a sequential and regulated manner. Microneme and rhoptry proteins crucially participate in motility, invasion, and egress from infected cells. They first traffic through...
ORGANISM(S): Toxoplasma gondii 
2018-01-30 | PXD006235 | Pride
Protease substrate screen Positional proteomics Tails 
ProteomicsMurine CLPP protease substrate trapping in MEF cells
Classic susbtrate-trapping screen for ClpXP substrates using MEF cell lines overexpressing FLAG-tagged CLPP (WT), proteolytically inactive CLPP (TRAP) or vector control (NEG)
ORGANISM(S): Mus musculus (Mouse) 
2020-06-01 | PXD015399 | Pride
Interactor Mouse Cllp protease Substrate Trap experiment Cell line 
UnknownA Proposal for a Structural Model of the Feline Calicivirus Protease Bound to the Substrate Peptide under Physiological Conditions.
Not available
S-EPMC5524728 | biostudies-literature
UnknownQuantitative proteomics screen identifies a substrate repertoire of rhomboid protease RHBDL2 in human cells and implicates it in epithelial homeostasis.
Not available
S-EPMC5544772 | biostudies-literature
UnknownTwo-step functional screen on multiple proteinaceous substrates reveals temperature-robust proteases with a broad-substrate range.
Not available
S-EPMC8053189 | biostudies-literature
UnknownIdentification and biochemical characterization of small-molecule inhibitors of west nile virus serine protease by a high-throughput screen.
Not available
S-EPMC2533463 | biostudies-literature
UnknownOMA1 High-Throughput Screen Reveals Protease Activation by Kinase Inhibitors.
Not available
S-EPMC8604787 | biostudies-literature
ProteomicsTargeted quantification of octapeptide substrate of FII and FX
Proteases are crucial physiologic regulators of protein structure and function. While proteomic methods contributed extensively to protease characterization efforts, technical challenges remain in terms of throughput, scalability and large datasets of protease cleavages remain scarce. Here, we descr...
ORGANISM(S): Homo sapiens (Human) 
2021-02-04 | PXD020319 | Pride
High-throughput protease screen Substrates Blood coagulation proteases Specificity Entropy Allostery 
ProteomicsTAILS N-Terminomics and Proteomics Show Complex Regulation of Proteolytic Processing by O-glycosylation
Proteolytic processing is an irreversible post-translational modification functioning as a ubiquitous regulator of cellular activity. Protease activity is tightly regulated by control of gene expression, compartmentalisation of enzyme and substrate, zymogen activation, enzyme inactivation, and subst...
ORGANISM(S): Homo sapiens (Human) 
2018-10-08 | PXD009453 | Pride
Human Lc-msms Degradomics O-glycoproteomics Tails 
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