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Nilaparvata lugens, or the brown planthopper, is one of the most notorious pest insects of cultured rice, and a model for hemimetabolous development. Recently, the N-glycome of N. lugens was explored throughout post-embryonic development and reproductive stages, which revealed differential protein N...
ORGANISM(S): Nilaparvata lugens 
2020-01-16 | PXD013657 | Pride
N-terminal (Nt) acetylation, catalyzed by N-terminal acetyltransferases (NATs), has emerged as an important co-translational modification in eukaryotes, and involves the transfer of the acetyl moiety from acetyl-CoA (Ac-CoA) to the α-amino group of a nascent polypeptide. Here, we report the first gl...
ORGANISM(S): Saccharomyces cerevisiae (Baker's yeast) 
2018-09-07 | PXD004326 | Pride
N-terminal acetylation is a conserved protein modification among eukaryotes, and the yeast Saccharomyces cerevisiae is a valuable model system for studying this modification. The enzymes responsible for the bulk of protein N-terminal acetylation in S. cerevisiae are the N-terminal acetyltransferases...
ORGANISM(S): Saccharomyces cerevisiae (Baker's yeast) 
2023-01-26 | PXD039544 | Pride
Co-translational N-terminal (Nt-) acetylation of nascent polypeptides is catalyzed by N-terminal acetyltransferases (NATs). The very N-terminal amino acid sequence is the major factor determining whether or not a given protein is Nt-acetylated. In humans, six different NATs, denoted NatA-NatF, are i...
ORGANISM(S): Saccharomyces cerevisiae (Baker's yeast) 
2015-05-29 | PXD001437 | Pride
To understand the impact of alternative translation initiation on a proteome, we performed the first large-scale study of protein turnover rates in which we distinguish between N-terminal proteoforms pointing to translation initiation events. Using pulsed SILAC combined with N-terminal COFRADIC we m...
ORGANISM(S): Homo sapiens (Human) 
2013-03-14 | PXD002091 | Pride
N-glycosylation is one of the most abundant and conserved protein modifications in eukaryotes. This modification serves various important functions, such as protein folding and cellular attachment, but also modulation of a protein’s function. Recently, it has been show...
ORGANISM(S): Buchnera aphidicola subsp. Acyrthosiphon pisum (Acyrthosiphon pisum symbiotic bacterium) Drosophila melanogaster (Fruit fly) Tetropium castaneum 
2018-06-18 | PXD008745 | Pride
N-terminal COFRADIC sorting of a Jurkat proteome
ORGANISM(S): Homo sapiens (Human) 
2011-08-01 | PRD000336 | Pride
Proteogenomics is a research field where proteome data is used to improve gene annotation. To achieve this, customized protein databases are constructed to match proteomic data. We perform a proteogenomic analysis using N-terminal COFRADIC data in order to identify novel translational initiation sta...
ORGANISM(S): Arabidopsis thaliana (Mouse-ear cress) 
2017-04-24 | PXD004896 | Pride
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 | PXD039392 | Pride
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 | PXD039171 | Pride
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