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N-terminal acetylation is one of the most abundant protein modifications in eukaryotes and is catalysed in humans by seven N-terminal acetyltransferases. AtNAA60 is localized in vivo at the plasma membrane by an α-helical membrane anchor at its C-terminus. In this study, we investigated the Arabidop...
ORGANISM(S): Escherichia coli 
2020-07-15 | PXD016533 | Pride
N-terminal acetylation (NTA) is one of the most abundant protein modifications in eukaryotes and is catalysed in humans by seven N-acetyltransferases. AtNAA60 localizes to the plasma membrane in vivo by an α-helical membrane anchor at its C-terminus. In this study, we investigated the Arabidopsis th...
ORGANISM(S): Arabidopsis thaliana (Mouse-ear cress) 
2020-07-15 | PXD016494 | Pride
The project was aimed at identifying the N-terminus of a truncated form of SLX4 (termed SLX4Nter) in HeLa KO30 cells. The HeLa KO30 cell line comes from a clone of HeLa Flp-In T-Rex cells (termed FITo) obtained through a CRISPR-Cas9 approach using commercially available plasmids from Santa Cruz Biot...
ORGANISM(S): Homo sapiens (Human) 
2022-02-16 | PXD029062 | Pride
N-terminal acetylation (NTA) is one of the most abundant protein modifications in eukaryotes and is catalysed in humans by seven N-acetyltransferases. In this study, we investigated the Arabidopsis thaliana NatB catalytic (NAA20) and auxiliary subunit (NAA25) and their influence on protein N-termina...
ORGANISM(S): Arabidopsis thaliana (Mouse-ear cress) 
2019-11-21 | PXD016209 | Pride
Protein acetylation is a universally conserved modification occurring on N-termini (N-Terminal acetylation, NTA). Although recent reports indicate that NTA occur frequently in plant plastids, little is known about the machinery involved in plastid acetylation and why these modifications are that fre...
ORGANISM(S): Escherichia coli 
2020-07-13 | PXD016205 | Pride
Reference dataset used for the development of the EnCOUNTEr tool to both (i) score all characterized peptides using discriminant parameters to evidence mature protein N-termini and (ii) determine the N-terminus acetylation yield for the most reliable ones.
ORGANISM(S): Arabidopsis thaliana (Mouse-ear cress) 
2017-03-14 | PXD005720 | Pride
A proteome-wide analysis was performed in Escherichia coli to identify the impact on protein N-termini of the antibiotic actinonin specifically inhibiting peptide deformylase (PDF). A new strategy and tool suite (SILProNaQ) was employed to provide large scale N-terminus acetylation yield quantitatio...
ORGANISM(S): Escherichia coli 
2015-07-21 | PXD002012 | Pride
Acetylation of lysine is a highly dynamic and reversibly regulated post-translational modification (PTM), which changes protein function in multiple ways [1]. As one of the most common PTMs to proteins in both eukaryotes and prokaryotes [1, 2], lysine acetylation occurred on either the α-amino group...
ORGANISM(S): Camellia sinensis 
2018-11-30 | PXD008931 | Pride
A proteome-wide analysis was performed in Escherichia coli to identify the impact on protein N-termini of the antibiotic actinonin specifically inhibiting peptide deformylase (PDF). A new strategy and tool suite (SILProNaQ) was employed to provide large scale N-terminus acetylation yield quantitatio...
ORGANISM(S): Escherichia coli 
2015-07-22 | PXD001983 | Pride
N-terminal acetylation is one of the most abundant protein modifications in eukaryotes and is catalysed in humans by seven N-terminal acetyltransferases. AtNAA50 interreact with the NatA complex (NAA10 and NAA15) to form the NatE complex. In this study, we investigated the activity of this catalytic...
ORGANISM(S): Escherichia coli 
2020-07-15 | PXD017767 | Pride
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