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An extended ChaFRADIC workflow was applied to analyze the N-terminal proteome of Arabidopsis thaliana seedlings. Using iTRAQ protein labeling, a multi-enzyme digestion approach including trypsin, GluC, and subtilisin, a total of 200 μg per enzyme were used, and only 1/3 of each ChaFRADIC-enriched fr...
ORGANISM(S): Arabidopsis thaliana (Mouse-ear cress) 
2015-07-21 | PXD001855 | Pride
Most MS-based workflows for N-terminal protein sequence analysis rely on the modification of primary amines at the protein N-terminus and lysine residues, in many cases through dimethylation. However, incomplete dimethyl labeling and undesired side reactions have been reported previously and were al...
ORGANISM(S): Bos taurus (Bovine) Escherichia coli Equus caballus (Horse) 
2026-08-17 | PXD081064 | Pride
In this study, we faced the challenge of deciphering a protein that has been designed and expressed by E.coli in such a way that the amino acid sequence encodes two concatenated English sentences. The sequence carried unknown modifications and cannot be found online. The letters ‘O’ and ‘U’ are both...
ORGANISM(S): Escherichia coli 
2020-05-26 | PXD012015 | Pride
The human N-terminal acetyltransferase E (NatE) including its associated NatA co-translationally acetylates the N-terminus of about 40-60% of the proteome to mediate diverse biological processes including protein half-life, localization and protein interaction. In eukaryotes, the NatE complex contai...
ORGANISM(S): Homo sapiens (Human) 
2020-03-13 | PXD017031 | Pride
The impact of NatC subunits NAA30, NAA35 and NAA38 on the human N-terminal acetylome. Analysis of HAP1 WT, NAA30 KO, NAA35 KO and NAA38 KO cells
ORGANISM(S): Homo sapiens (Human) 
2023-09-13 | PXD034992 | Pride
Abstract still has to be written. The obtained peptide mixtures were introduced into an LC-MS/MS system, the Ultimate 3000 (Dionex, Amsterdam, The Netherlands) in-line connected to an LTQ Orbitrap XL mass spectrometer (Thermo Fisher Scientific, Bremen, Germany). Samples were first loaded on a trapp...
ORGANISM(S): Homo Sapiens (ncbitaxon:9606) 
2019-03-13 | MSV000083564 | MassIVE
N-terminal proteoforms stem from the same gene but differ at their N-terminus, and most of these are found to be truncated, though some are N-terminally extended caused by ribosomes starting translation from codons in the annotated 5’UTR, and/or carry modified N-termini different from those of the c...
ORGANISM(S): Homo sapiens (Human) 
2023-06-08 | PXD039085 | Pride
Ultraviolet photodissociation (UVPD) has emerged as a powerful alternative to conventional collision-induced dissociation (CID) for peptide and protein sequencing in mass spectrometry–based proteomics. However, UVPD efficiency depends on the presence of UV-absorbing chromophores within analytes.The ...
ORGANISM(S): Homo sapiens (Human) 
2026-06-08 | PXD075227 | Pride
Ribosome profiling revealed translation outside of canonical coding sequences (CDSs) including translation of short upstream open-reading frames (ORFs), long non-coding RNAs, ORFs in UTRs or ORFs in alternative reading frames. Ribo-seq but also bioinformatics-based prediction and RNA-sequencing repo...
ORGANISM(S): Homo sapiens (Human) 
2022-07-12 | PXD030601 | Pride
The field of proteomics has evolved hand-in-hand with technological advances in LC-MS/MS systems, now enabling the analysis of very deep proteomes in a reasonable time. However, most applications do not deal with full cell or tissue proteomes, but rather with restricted sub-proteomes relevant for th...
ORGANISM(S): Saccharomyces cerevisiae (Baker's yeast) 
2015-05-07 | PXD001695 | Pride
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