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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
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
Elucidating the true physiological functions of granzymes has been challenging since the origin of the granzyme studied, the use of non-physiological granzyme concentrations and the interspecies use of granzymes, with extrapolation of all these data to orthologous granzymes has led to inconsistencie...
ORGANISM(S): Homo sapiens (Human) 
2015-09-30 | PXD000570 | Pride
Small molecules not only represent cellular building blocks and metabolic intermediates, but also regulatory ligands and signaling molecules that interact with proteins. Although these interactions affect cellular metabolism, growth, and development, they have been largely understudied. Herein, we d...
2018-07-19 | MTBLS94 | MetaboLights
Complementary positional proteomics of human and mouse granzyme M treated K-562 lysates
2012-05-23 | PRD000347 | Pride
Identification of protease substrates and determination of their specificities can provide important insights into their function. In the past decade, several proteomic approaches for identification of protease cleavage sites were developed, each relying on various strategies for peptide labelling a...
ORGANISM(S): Homo sapiens (Human) 
2015-02-10 | PXD001553 | Pride
Addressing the elusive specificity of cysteine cathepsins, which in contrast to caspases and trypsin-like proteases lack strict specificity determining P1 pocket, was calling for innovative approaches. Proteomic analysis of cell lysates with human cathepsins K, V, B, L, S, and F identified 30,000 cl...
ORGANISM(S): Homo sapiens (Human) 
2023-03-29 | PXD041185 | 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
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