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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 
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 
UnknownImproved sensitivity mass spectrometric detection of eicosanoids by charge reversal derivatization.
Not available
S-EPMC2959116 | biostudies-literature
ProteomicsHelical superstructures between amyloid and collagen VI in heart derived fibrils from a patient with Light Chain Amyloidosis
We investigated the N- and C-terminome of the LCs proteoforms in fibrils extracted from the hearts of a patient affected by AL amyloidosis, using a proteomic approach based on N- and C-terminal residues derivatization, followed by mapping of fragmentation sites on the structures of fibrillar LCs
ORGANISM(S): Homo sapiens (Human) 
2024-07-02 | PXD049301 | Pride
Amyloid fibrils  fragmentation sites  immunoglobulin light chains 
UnknownDevelopment of a sensitive and quantitative method for the identification of two major furan fatty acids in human plasma.
Not available
S-EPMC7112149 | biostudies-literature
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