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ProteomicsCharacterization of the Clostridioides difficile 630Δerm putative Pro-Pro endopeptidase CD1597
Clostridioides difficile is the leading cause of antibiotic-associated infections worldwide. Within the host, C. difficile can transition from a sessile to a motile state by secretion of PPEP-1, which releases the cells from the intestinal epithelium by cleaving adhesion proteins. PPEP-1 belongs to ...
ORGANISM(S): Peptoclostridium difficile (strain 630) (Clostridium difficile) 
2024-05-27 | PXD052347 | Pride
Tmtpro Proteomics Sporulation Clostridioides difficile Proteases Pro-pro endopeptidases 
TranscriptomicsHC-Pro silencing suppressor significantly alters the gene expression profile in tobacco leaves and flowers
Agilent 4x44k tobacco micro array of wild type tobacco, empty vector control, and HC-Pro transgenic tobacco plants. Both 1-month old leaves and flowers were analyzed. Three biological replicates were performed of each sample.
ORGANISM(S): Nicotiana tabacum 
2011-08-10 | E-MEXP-3105 | biostudies-arrayexpress
ProteomicsNon-prime- and Prime-side Profiling of Pro-Pro Endopeptidase Specificity Using Synthetic Combinatorial Peptide Libraries and Mass Spectrometry
A group of bacterial proteases, the Pro-Pro endopeptidases (PPEPs), possess the unique ability to hydrolyze proline-proline bonds in proteins. Since a protease’s function is largely determined by its substrate specificity, methods that can extensively characterize substrate specificity are valuable ...
ORGANISM(S): Anoxybacillus tepidamans Paenibacillus alvei Peptoclostridium difficile (strain 630) (Clostridium difficile) 
2025-11-11 | PXD050236 | Pride
Clostridioides difficile Paenibacillus alvei Ppep Protease Specificity Pro-pro endopeptidase Anoxybacillus tepidamans Lc-ms/ms 
ProteomicsBiochemical and structural characterization of PPEP-3 from Geobacillus thermodenitrificans
The members of the group of Pro-Pro endopeptidases (PPEPs) are secreted bacterial endoproteases that display a unique preference for hydrolyzing their substrates between two proline residues. The active site cleft of PPEPs accommodates the six substrate residues P3 to P3’, and the interactions betwe...
ORGANISM(S): Geobacillus thermodenitrificans 
2025-11-11 | PXD061585 | Pride
Geobacillus thermodenitrificans Macromolecular x-ray crystallography Zinc metallopeptidase Mass spectrometry Substrate specificity Pro-pro endopeptidase-3 
TranscriptomicsPBECs stimulated with pro-inflammatory cytokines and P. aeruginosa
Comparison of libraries derived from primary human bronchial epithelial cells which are [i] unstimulated, [ii] stimulated with the pro-inflammatory cytokines IL1beta and TNFalpha and [iii] stimulated with heat-inactivated Pseudomonas aeruginosa (strain PAO1). Keywords: other
ORGANISM(S): Homo sapiens 
2005-02-02 | E-GEOD-2056 | biostudies-arrayexpress
UnknownCharacterization of the Clostridioides difficile 630Δerm putative Pro-Pro endopeptidase CD1597.
Not available
S-EPMC11460543 | biostudies-literature
ProteomicsPBRM1-deficient PBAF complexes target de novo genomic loci to activate pro-survival genes in clear cell renal cell carcinoma (PBRM1 dataset)
PBRM1 is lost in 40% of clear cell renal cell carcinomas (ccRCC) and the combined loss of VHL and PBRM1 drives ccRCC tumorigenesis. PBRM1 is an accessory subunit of the PBAF subclass of the SWI/SNF chromatin remodeler and despite its well-established role as a tumor suppressor, we have limited under...
ORGANISM(S): Homo Sapiens (human) 
2021-07-24 | PXD020554 | JPOST Repository
ProteomicsPBRM1-deficient PBAF complexes target de novo genomic loci to activate pro-survival genes in clear cell renal cell carcinoma (BRG1 dataset)
PBRM1 is lost in 40% of clear cell renal cell carcinomas (ccRCC) and the combined loss of VHL and PBRM1 drives ccRCC tumorigenesis. PBRM1 is an accessory subunit of the PBAF subclass of the SWI/SNF chromatin remodeler and despite its well-established role as a tumor suppressor, we have limited under...
ORGANISM(S): Homo Sapiens (human) 
2021-07-24 | PXD020553 | JPOST Repository
UnknownProduction of authentic SARS-CoV M(pro) with enhanced activity: application as a novel tag-cleavage endopeptidase for protein overproduction.
Not available
S-EPMC7094453 | biostudies-literature
ProteomicsIn-depth specificity profiling of Pro-Pro endopeptidases (PPEPs) using combinatorial synthetic peptide libraries
Proteases comprise the class of enzymes that catalyze the hydrolysis of peptide bonds, thereby playing a pivotal role in many aspects of life. The amino acids surrounding the scissile bond determine the susceptibility towards protease-mediated hydrolysis. A detailed understanding of the cleavage spe...
ORGANISM(S): Paenibacillus alvei DSM 29 Geobacillus stearothermophilus Clostridioides difficile 
2023-08-01 | PXD038277 | Pride
Pro-pro endopeptidase Specificity profiling Mass spectrometry (ms) Ppep Synthetic peptide libraries Substrate specificity High-performance liquid chromatography (hplc) Fret peptides Metalloprotease 
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