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ProteomicsSystematic optimization of C-TAILS approach for deep screening of C-terminomics
It is well known that protein C-termini play important roles in various biological processes, and thus the precise characterization of C-termini is essential for fully elucidating protein structure and understanding protein functions. Although many efforts have been made in the fields during the lat...
ORGANISM(S): Escherichia coli 
2015-09-15 | PXD002409 | Pride
Protein c-termini Acetylation Scii 
ProteomicsSCX, 18O-labeling and charge reversal for C-terminomics
The proteome wide, mass spectrometry based identification of protein C-termini is hampered by factors such as poor ionization efficiencies, low yields in labeling strategies or the need for enrichment procedures. We present a bottom-up proteomics workflow to identify protein C-termini utilizing a co...
ORGANISM(S): Saccharomyces cerevisiae (Baker's yeast) 
2019-06-20 | PXD013486 | Pride
Lc-ms Charge-reversal derivatization C-terminomics 
ProteomicsLysargiNase and Chemical Derivatization Based Strategy for 2 Facilitating In-Depth Profiling of C‑Terminome
we developed a new method for C-terminomics, in which LysargiNase and chemical derivatization were integrated to increase the identification confidence.
ORGANISM(S): Homo Sapiens 
2019-12-16 | PXD016756 |
ProteomicsPBC, an easy and efficient strategy for high-throughput protein C-terminome profiling
So far, high-efficiency and high-throughput analysis of C-terminal peptides is still full of challenges. In order to make the chemical derivatization-based strategies more practical and efficient, in this study we developed a new method, named 2-pyridinecarboxaldehyde (2PCA) and biotin labeling bas...
ORGANISM(S): Homo Sapiens 
2022-08-01 | PXD035645 |
ProteomicsC-terminomics E. coli - C-terminal charge-reversal derivatization and parallel use of multiple proteases facilitates identification of protein C-termini by C-terminomics
The identification of protein C-termini in complex proteomes is challenging due to the poor ionization efficiency of the carboxyl group. Amidating the negatively charged C-termini with ethanolamine (EA) has been suggested to improve detection of C-terminal peptides and allows for a directed depletio...
ORGANISM(S): Escherichia coli 
2016-03-11 | PXD003342 | Pride
Cid Hcd Etd C-terminus Derivatization 
UnknownC-terminomics screen for natural substrates of cytosolic carboxypeptidase 1 reveals processing of acidic protein C termini.
Not available
S-EPMC4288253 | biostudies-literature
ProteomicsOne-step N-terminomics based on isolation of protein N-terminal peptides from LysargiNase digests by tip-based strong cation exchange chromatography
Large-scale isolation of protein N-terminal peptides from LysargiNase digests was achieved by one-step strong cation exchange chromatography with disposable and parallel-processable pipette-tip columns. Novel cleavage sites for signal or transit peptides and non-canonical translation initiation site...
ORGANISM(S): Homo Sapiens (human) 
2024-08-13 | PXD048917 | JPOST Repository
ProteomicsOne-step Isolation of Protein C-terminal Peptides from Protease-digested Proteins by Metal Oxide-based Ligand Exchange Chromatography
We have developed a one-step method to isolate protein C-terminal peptides from V8-digested proteins by metal oxide-based ligand-exchange (MOLEX) chromatography. V8 protease cleaves the C-terminal side of Asp and Glu, and the resulting digested peptide has two carboxy groups at the C-terminus, where...
ORGANISM(S): Homo Sapiens (human) 
2021-12-28 | PXD027960 | JPOST Repository
ProteomicsDipeptidyl peptidase DPF-3 is a gatekeeper of microRNA Argonaute compensation in animals
MicroRNAs (miRNAs) are essential regulators involved in multiple biological processes. To achieve their gene repression function, they are loaded in miRNA-specific Argonautes to form the miRNA-induced silencing complex (miRISC). Mammals and C. elegans possess more than one paralog of miRNA-specific ...
ORGANISM(S): Caenorhabditis elegans 
2025-03-06 | PXD055867 | Pride
Proteomics Dpf-3 Microrna Argonautes Lc-ms 
ProteomicsPositional proteomics identification of the natural substrates of cytosolic carboxypeptidases
Cytosolic carboxypeptidases (CCPs) constitute a new subfamily of M14 metallocarboxypeptidases associated to axonal regeneration and neuronal degeneration, amongst others. CCPs are deglutamylating enzymes, able to catalyze the shortening of polyglutamate side-chains and the gene-encoded C-termini of ...
ORGANISM(S): Homo sapiens (Human) 
2014-12-02 | PXD000834 | Pride
Degradomics c-terminomics carboxypeptidase 
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