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Histone post-translational modifications (PTMs) alter chromatin dynamics and contribute to the regulation of gene expression in health and disease. Mass spectrometry-based analysis is the gold-standard for histone PTM analysis, but it remains constrained by inefficient sample preparation workflows r...
ORGANISM(S): Homo sapiens (Human) Rattus norvegicus (Rat) 
2026-06-20 | PXD073683 | Pride
High specificity and ease of use make trypsin the most used enzyme in proteomics. Proteases with complementary cleavage specificity to trypsin have been applied to obtain additional data. However, use of proteases with broad specificity proved especially challenging. In this work, we analyzed the ch...
ORGANISM(S): Schizosaccharomyces pombe OY26 
2021-06-07 | PXD017321 | Pride
Human antibodies are heterogeneous molecules, primarily due to clonal sequence variations. Analytical techniques to assess antibody levels quantitatively, like ELISA assays, lack the power to determine abundances at the clonal level. Recently, we introduced an LC-MS-based approach that can distingui...
ORGANISM(S): Homo Sapiens (ncbitaxon:9606) 
2023-08-17 | MSV000092676 | MassIVE
Staphylococcus aureus is a gram-positive opportunistic pathogen that has colonized nearly 30% of the human population and can cause life-threatening infections. The antibiotic treatment of S. aureus infection is often hindered by several resistances expressed by the pathogen, and therefore alternati...
ORGANISM(S): Staphylococcus Arlettae (ncbitaxon:29378) 
2024-10-14 | MSV000096077 | MassIVE
S. pombe proteome digested separately by four proteases and analyzed with an LTQ-Orbitrap Velos with a data-dependent decision tree method.
2013-12-23 | MSV000078516 | MassIVE
In proteome studies, the application of alternative proteases, exclusively or in addition to trypsin, often increases protein sequence or proteome coverage. It has recently been shown that, in particular, the analysis of small proteins benefits from such multi-protease approaches. In the accompanyin...
ORGANISM(S): Bacillus subtilis subsp. subtilis str. 168 
2026-01-23 | PXD062213 | Pride
Palaeoproteomics of skeletal tissues has the potential to provide new insights into the evolutionary relationships between globally distributed hominin fossils across the Pleistocene. The use of alternative or additional proteases has the potential to increase both proteome size and protein. However...
ORGANISM(S): Homo Equidae 
2020-10-13 | PXD018264 | Pride
Ancient skeletal proteomes are increasingly utilised for phylogenetic and evolutionary analysis. These proteomes are, however, often small and with low sequence coverage. We expand on previous observations which have shown that parallel digestion of Pleistocene skeletal proteomes increases proteome ...
ORGANISM(S): Bos taurus (Bovine) Equus caballus (Horse) 
2024-03-06 | PXD047069 | Pride
Mass spectrometry-based proteomics now routinely enables identification of over 10,000 human proteins from a single sample. However, proteins are typically identified by peptide sequences representing about 20% of all proteinogenic amino acids encoded in the transcriptome. Deeper protein sequencing ...
ORGANISM(S): Homo Sapiens (ncbitaxon:9606) 
2021-02-24 | MSV000086944 | MassIVE
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