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ProteomicsCharacterization of LysargiNase for use in phosphoproteomics experiments, part 1
Use of parallel digest with LysargiNase (former name: ulilysin) and trypsin to cover complementary phosphosites / characterization of phospho-motifs preferentially identified by each protease
ORGANISM(S): Homo sapiens (Human) 
2014-12-16 | PXD001121 | Pride
Phosphopeptides Mda-mb 231 Lysarginase Human Trypsin 
ProteomicsCharacterization of LysargiNase for use in phosphoproteomics experiments, partII
Use of parallel digest with LysargiNase and trypsin to cover complementary phosphosites / characterization of phospho-motifs preferentially identified by each protease
ORGANISM(S): Homo sapiens (Human) 
2014-12-16 | PXD001114 | Pride
Phosphopeptides Silac Lysarginase Human Trypsin Mda-mb 231 Pma stimulation 
ProteomicsLysargiNase cleavage specificity characterization
Determination of LysargiNase and tryptic ckeavage efficiency at dimethylated Lys residues
ORGANISM(S): Escherichia coli 
2014-12-16 | PXD001379 | Pride
E.coli Dimethyl-lys Lysarginase Trypsin 
ProteomicsMirroring the charged termini; ETD/HCD fragmentation characteristics of LysargiNase and tryptic peptides and their benefits for peptide sequencing in proteomics
A key step in proteomics is the digestion of proteins into peptides, so far largely done by using trypsin. Tryptic digestion leads to peptides that in ESI-MS attain predominantly two charges, via protonation at the free N-terminus and at the C-terminal basic residue Arginine or Lysine. These peptide...
ORGANISM(S): Homo sapiens (Human) 
2016-12-02 | PXD004447 | Pride
Fragmentation Etd Hcd Lysarginase Orbitrap Phosphoproteomics Trypsin 
ProteomicsThe use of LysargiNase complementary to trypsin in large scale phosphoproteome study for unambiguous phosphosite localization
Understanding of kinase-guided signaling pathways requires identification and analysis of phosphorylation sites. Mass spectrometry (MS)-based phosphoproteomics is a rapid and highly sensitive approach for high-throughput identification of phosphorylation sites. However, the exact localization of pho...
ORGANISM(S): Homo sapiens (Human) 
2020-05-22 | PXD011178 | Pride
Phosphoproteome Phosphosite localization Lysarginase 
ProteomicsLysargiNase and tryptic digest of MDA-MB 231 cell lysates
Comparison of peptide properties in proteomes digested with LysargiNase in comparison to trypsin
ORGANISM(S): Homo sapiens (Human) 
2014-12-16 | PXD001113 | Pride
Human Mda-mb 231 Cell line Lc-ms/ms 
ProteomicsSpecificity profiling of LysargiNase in comparison to trypsin
Protease cleavage site preferences of LysargiNase (former name: ulilysin) and trypsin were tested using proteome-derived peptide libraries (Schilling et al Nature Protocols 2011)
ORGANISM(S): Escherichia coli 
2014-12-16 | PXD001122 | Pride
Protease Pics Sequence specificity 
ProteomicsE. coli mirror LC-MS/MS - Precision de novo peptide sequencing using mirror proteases of Ac-LysargiNase and trypsin for large-scale proteomics
Precision de novo peptide sequencing using mirror proteases of Ac-LysargiNase and trypsin for large-scale proteomicsPrecision de novo peptide sequencing using mirror proteases of Ac-LysargiNase and trypsin for large-scale proteomics
ORGANISM(S): Escherichia coli 
2019-01-11 | PXD008688 | Pride
Mirror spectrum pairs E. coli Lc-ms/ms 
ProteomicsCharacterization of LysargiNase peptide fragmentation
Comparison of Lyarginase and tryptic digests with regard to fragmentation behaviour/effect of inclusing a ion in peptide assignment scoring
ORGANISM(S): Escherichia coli 
2014-12-16 | PXD001378 | Pride
E.coli Lysarginase 
ProteomicsLysargiNase Enhances the Protein Identification on FFPE Samples
Formalin-Fixed Paraffin-Embedded (FFPE) samples are treasure for proteomic studies of disease. However, their usage is hampered for proteomics study because of the crosslink among proteins, and protein vs nucleic acid. Even worse, other covalent chemical modifications like methylation introduced by ...
ORGANISM(S): Mus Musculus 
2019-02-15 | PXD012738 |
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