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ProteomicsHydrophobic tagging-assisted N-termini enrichment (HYTANE) for in-depth N-terminome analysis
The analysis of protein N-termini is of great importance for understanding the protein function and elucidating the proteolytic processing. Herein, we develop a negative enrichment strategy, termed as hydrophobic tagging-assisted N-termini enrichment (HYTANE) to achieve a global N-terminome analysis...
ORGANISM(S): Homo sapiens (Human) Saccharomyces cerevisiae (Baker's yeast) 
2016-08-19 | PXD004690 | Pride
Sacchoromyces cerevisiae Jurkat N-termini Caspase 
UnknownHYTANE-Identified Latrophilin-3 Cleavage by Meprin β Leads to Loss of the Interaction Domains.
Not available
S-EPMC11976865 | biostudies-literature
ProteomicsIn vitro characterization of caspase-3 cleavage sites by LATE and HYATNE
Proteins' N-termini contain information about their biochemical properties and functions, and they can undergo co- or post-translational modifications, as well as be processed by proteases. To expand the coverage of the N-terminome, we have developed LATE (LysN Amino Terminal Enrichment), a method t...
ORGANISM(S): Homo sapiens (Human) 
2023-06-27 | PXD036593 | Pride
Late Hytane Lysn Peptidyl-lys metalloendopeptidase n-terminomics Caspase-3 
ProteomicsCell-based characterization of caspase-3 cleavage sites by LATE and HYATNE
Proteins' N-termini contain information about their biochemical properties and functions, and they can undergo co- or post-translational modifications, as well as be processed by proteases. To expand the coverage of the N-terminome, we have developed LATE (LysN Amino Terminal Enrichment), a method t...
ORGANISM(S): Homo sapiens (Human) 
2023-06-27 | PXD036648 | Pride
Late Hytane Abt199 Lysn Peptidyl-lys metalloendopeptidase n-terminomics Caspase-3 
ProteomicsAspartyl Protease 5 matures virulence factors found at the host-parasite interface in Toxoplasma gondii
N-terminome analysis of WT and ASP5 KO Toxoplasma parasites.
ORGANISM(S): Toxoplasma gondii Toxoplasma gondii ME49 
2018-10-15 | PXD008574 | Pride
N-terminome Effector Asp5 Tails Toxoplasma 
ProteomicsTargeted approach to determine the impact of cancer-associated protease variants
Several mechanisms of cancer progression, from tumour onset to metastasis, critically involve proteolytic activity. Studying the role of proteases in cancer, it is important to consider single nucleotide variants (SNVs) affecting the active site of proteases, that might impact cleavage specificity, ...
ORGANISM(S): Homo sapiens (Human) 
2025-05-06 | PXD048501 | Pride
Snvs Meprin β Proteases Cancer Migration Spheroids Cancer-associated variants Cleavage specificity N-terminomics Organotypic brain slices 
ProteomicsN-terminome analyses of the intramembrane-cleaving protease SPPL3
The intramembrane protease SPPL3 can specifically cleave select Golgi enzymes, enabling their secretion and concomitantly altering global cellular glycosylation, yet the entire range of Golgi glycan-modifying enzymes cleaved by SPPL3 under physiological conditions remains to be defined. Here, we est...
ORGANISM(S): Homo sapiens (Human) 
2022-03-17 | PXD028769 | Pride
Hek293 Label-free Hela Sppl3 N-terminomics 
ProteomicsProteolytic processing of galectin-3 is crucial for host microbiome homeostasis
To identify relevant substrates for meprin α/β heterodimers, we applied mass spectrometry-based N-terminomics of mouse colon tissue as well as of human Caco-2 cells and identified galectin-3 as a novel intestinal substrate. The proteolytic processing of galectin-3 by meprin α/β heterodimers plays a ...
ORGANISM(S): Mus musculus (Mouse) 
2023-05-10 | PXD037000 | Pride
Lc-ms Meprin N-terminomics 
ProteomicsIn vitro sheding activity of ADAM10
Investigation of the shading activity of the recombinant catalytic domain of ADAM10
ORGANISM(S): Homo sapiens (Human) 
2023-05-17 | PXD040511 | Pride
Adam10 app alzheimer’s disease 
ProteomicsN-terminal acetylation of yeast NAT-A mutants
Protein-protein interactions are fundamental to all cellular activities, with the ribosome increasingly recognized as a central platform steering the dynamics of nascent-chain interactions. In our focus on conserved N-terminal acetyltransferases (NATs), we identified distinct co-translational assemb...
ORGANISM(S): Saccharomyces cerevisiae (Baker's yeast) 
2024-06-22 | PXD048082 | Pride
N-terminal acetylation Naa15 Naa10 Co-translational assembly Terminomics 
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