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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
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 (Human) 
2016-12-23 | PXD000551 | 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
Differential complementary positional proteomics of human granzyme B treated K-562 lysates
ORGANISM(S): Homo sapiens (Human) 
2010-05-19 | PRD000229 | Pride
Eukaryotic cells maintain homeostasis of their outer membrane by controlled internalization of lipid and protein constituents by endocytosis (Kaksonen & Roux, Nat Rev Mol Cell Biol. 2018). Endocytosis is evolutionary conserved and utilizes similar structural folds. How these structural folds are com...
ORGANISM(S): Arabidopsis thaliana (Mouse-ear cress) 
2025-11-06 | PXD056680 | Pride
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