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We here apply the COmbined FRActional DIagonal Chromatography (COFRADIC) technology to enrich for ubiquitinated peptides and identify sites of ubiquitination by mass spectrometry. Our technology bypasses the need to ectopically overexpress tagged variants of ubiquitin and the use of sequence-biased ...
ORGANISM(S): Homo sapiens (Human) 
2016-07-08 | PXD000934 | Pride
We here apply the COmbined FRActional DIagonal Chromatography (COFRADIC) technology to enrich for ubiquitinated peptides and identify sites of ubiquitination by mass spectrometry. Our technology bypasses the need to ectopically overexpress tagged variants of ubiquitin and the use of sequence-biased ...
ORGANISM(S): Homo Sapiens (ncbitaxon:9606) 
2017-03-29 | MSV000080780 | MassIVE
The X-linked lethal Ogden syndrome was the first reported human genetic disorder associated with a mutation in an N-terminal acetyltransferase gene. The affected males harbour a Ser37Pro mutation in the gene encoding hNaa10, the catalytic subunit of NatA, themajor human NAT. In order to understand t...
ORGANISM(S): Homo sapiens (Human) 
2016-04-12 | PXD001282 | Pride
N-terminal COFRADIC analysis of cathespine K, L and S to obtain the substrate specificity profile of these cysteine cathepsins.
ORGANISM(S): Homo sapiens (Human) 
2015-02-10 | PXD001536 | 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
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 acetylation is a major and vital protein modification catalysed by N-terminal acetyltransferases (NATs). NatF or Nα-acetyltransferase 60 (Naa60) was recently identified as a NAT in higher eukaryotes. Here, we found that Naa60 differs from all other known NATs by its Golgi localization. A ...
ORGANISM(S): Homo sapiens (Human) 
2019-06-04 | PXD001155 | Pride
N-terminal acetylation is one of the most common protein modifications in eukaryotes, with emerging roles in regulating protein quality and stoichiometry and targeting and complex formation. The NatC complex is one of the three major N-terminal acetyltransferases (NATs). Here, we partially defined t...
ORGANISM(S): Homo sapiens (Human) 
2016-10-05 | PXD000930 | 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
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