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ProteomicsHuman Dental Pulp TAILS N-terminomics
We report the targeted analysis of the human dental pulp proteome and N-terminome using the positional proteomics technique TAILS, which allowed us to capture both naturally blocked and unblocked protein N-termini. Furthermore, by using a proteomically barely studied human tissue in combination with...
ORGANISM(S): Homo Sapiens (ncbitaxon:9606) 
2018-06-26 | MSV000082509 | MassIVE
ProteomicsHs_C-HPP_DentalPulpTails_N-terminomics
Hs_C-HPP, dental pulp proteome, TAILS technique
ORGANISM(S): Homo Sapiens (human) 
2015-12-31 | PAe005343 | PeptideAtlas
ProteomicsDeciphering changes to human platelet proteome and degradome during storage before transfusion
Proteases, and specifically metalloproteinases, have been linked to the loss of platelet function during storage before transfusion, albeit the mechanism remains unknown. We used a dedicated N-terminomics technique, multiplex iTRAQ-TAILS (Terminal Amine Isotope Labeling of Substrates), to characteri...
ORGANISM(S): Homo sapiens (Human) 
2014-10-24 | PXD000906 | Pride
Platelets Metalloproteinases Degradome Proteases Tails Human Ls-msms 
ProteomicsProteomic analysis of human alveolar bone
We optimised a sample preparation and analysis workflow for proteomic analysis of human alveolar bone. We compared the peptides and proteins extracted from bone by different buffers, then used a multi-enzyme, multi-search engine approach to increase proteome coverage.
ORGANISM(S): Homo sapiens (Human) 
2019-11-27 | PXD011524 | Pride
Human Bone Tails Shotgun Missing protein 
ProteomicsTAILS N-terminomics of the human dental pulp stroma and the odontoblast layer
We report the targeted analysis of the human dental pulp stroma and the odontoblast layer using the positional proteomics technique TAILS N-terminomics, which allowed us to capture both naturally blocked and unblocked protein N-termini, and to identify differences between e.g. the dental pulp proteo...
ORGANISM(S): Homo Sapiens (ncbitaxon:9606) 
2019-06-10 | MSV000083951 | MassIVE
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 
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 
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 
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 
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 
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