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MetabolomicsProteolytic-Resistant Self-Assembling Peptide Nanofibers Combat Specific Bacterial Infections via Trap-and-Kill

The rise in global antibiotic resistance highlights the urgent need for effective antimicrobial agents. Antimicrobial peptides (AMPs) offer a potential solution to combat bacterial resistance. However, key challenges remain in addressing the limitations of current peptide drugs and biomaterials, ...

2025-06-13 | MTBLS12424 | MetaboLights
ProteomicsProteolytic Cleavage Activates the Mitochondrial Isoform of TOP3A
The TOP3A gene encodes two isoforms, one targeted to the nucleus and one to mitochondria. Nuclear TOP3A functions as part of the BTRR complex to resolve double Holliday junctions during homologous recombination, while the mitochondrial isoform separates hemicatenated daughter mitochondrial DNA molec...
ORGANISM(S): Homo sapiens (Human) 
2025-10-01 | PXD064926 | Pride
Top3a Mitochondria Mitochondrial processing peptidase (mmp) Proteolytic cleavage product 
GenomicsProteolytic cleavage of Tie1 governs vascular response to inflammatory stimulations
Proteolytic cleavage of Tie1 governs vascular response to inflammatory stimulations
PRJNA1214222 | ENA
TranscriptomicsCleavage of NIK by the API2-MALT1 Fusion Oncoprotein Leads to Noncanonical NF-{kappa}B Activation
Proper regulation of nuclear factor κB (NF-κB) transcriptional activity is required for normal lymphocyte function, and deregulated NF-κB signaling can facilitate lymphomagenesis. We demonstrate that the API2-MALT1 fusion oncoprotein created by the recurrent t(11;18)(q21;q21) in mucosa-associated ly...
ORGANISM(S): Homo sapiens 
2011-01-30 | E-GEOD-25527 | biostudies-arrayexpress
ProteomicsMetalloprotease-mediated cleavage of CD95 Ligand: QTOF Xevo XS data
CD95 is a member of the TNF receptor superfamily that is ubiquitously expressed in healthy and pathological tissues. Stimulation of CD95 by its physiological ligand CD95L induces its oligomerization leading in turn to the transduction of either apoptotic or non-apoptotic signals. CD95L can exist as ...
ORGANISM(S): Homo sapiens (Human) 
2023-02-20 | PXD039211 | Pride
Cd95l Metalloprotease Proteolytic cleavage 
TranscriptomicsProteolytic cleavage of Tie1 governs vascular response to inflammatory stimulations
We here show that proteolytic cleavage of the Tie1 receptor evokes a vascular response to inflammatory stimulations such as TNFalpha and LPS. Resisting Tie1 cleavage reprogrammed EC gene networks, rendering them non-responsive to inflammatory stimulations.
ORGANISM(S): Mus musculus 
2026-07-24 | GSE287671 | GEO
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 
TranscriptomicsProteolytic cleavage by taspase1 and the regulation of the stability of MLL1
Chromosomal translocations of the Mixed-lineage leukemia 1 (MLL1) gene generate MLL-chimeras that drive pathogenesis of acute myeloid and lymphoid leukemia. The untranslocated MLL1 is a substrate for proteolytic cleavage by the endopeptidase, taspase1, however, the biological significance of MLL1 cl...
ORGANISM(S): Homo sapiens 
2019-01-02 | GSE90762 | GEO
ProteomicsTime-resolved analysis of proteolytic cleavage sites in Malate dehydrogenase by Trypsin.
A proteolytic cleavage experiment was performed with the protein Malate dehydrogenase (MDH) and Trypsin protease, to identify early cleavage sites in MDH. Various concentrations of Trypsin (5,000, 10,000 and 100,000 x diluted) were tested and early timepoints taken to detect only few cleavage sites...
ORGANISM(S): Sus scrofa domesticus (domestic pig) 
2024-09-20 | PXD047437 | Pride
Trypsin Mass spectrometry Malate dehydrogenase 
UnknownGenetically determined proteolytic cleavage modulates alpha7beta1 integrin function.
Not available
S-EPMC2602887 | biostudies-literature
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