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PXD010563

PXD010563 is an original dataset announced via ProteomeXchange.

Dataset Summary
TitleUoL_turnover_SRM (Holman et al. 2016)
DescriptionProtein turnover represents an important mechanism in the functioning of cells, with deregulated synthesis and degradation of proteins implicated in many diseased states. Therefore, proteomics strategies to measure, with high confidence, turnover rates are of vital importance to understanding many biological processes. In this study, the more widely used approach of non-targeted precursor ion signal intensity (MS1) quantification is compared to selected reaction monitoring (SRM), a data acquisition strategy that records data for specific peptides, to determine if improved quantitative data would be obtained using a targeted quantification approach. Using mouse liver as a model system, turnover measurement of four tricarboxylic acid cycle proteins was performed using both MS1 and SRM quantification strategies. SRM outperformed MS1 in terms of sensitivity and selectivity of measurement, allowing more confident determination of protein turnover rates. SRM data is acquired using cheaper and more widely available tandem quadrupole mass spectrometers, making the approach accessible to a larger number of researchers than MS1 quantification, which is best performed on high mass resolution instruments. SRM acquisition is ideally suited to focussed studies where the turnover of tens of proteins is measured, making it applicable in determining the dynamics of proteins complexes and complete metabolic pathways.
HostingRepositoryPeptideAtlas
AnnounceDate2018-07-25
AnnouncementXMLSubmission_2018-07-25_10:11:16.xml
DigitalObjectIdentifier
ReviewLevelPeer-reviewed dataset
DatasetOriginOriginal dataset
RepositorySupportSupported dataset by repository
PrimarySubmitterStephen Holman
SpeciesList scientific name: Mus musculus; NCBI TaxID: 10090;
ModificationListS-carboxamidomethyl-L-cysteine; 6x(13)C labeled L-lysine
InstrumentTSQ Vantage
Dataset History
RevisionDatetimeStatusChangeLog Entry
02018-07-25 10:08:47ID requested
12018-07-25 10:11:17announced
Publication List
Holman SW, Hammond DE, Simpson DM, Waters J, Hurst JL, Beynon RJ, Protein turnover measurement using selected reaction monitoring-mass spectrometry (SRM-MS). Philos Trans A Math Phys Eng Sci, 374(2079):(2016) [pubmed]
Keyword List
curator keyword: selected reaction monitoring, SRM, targeted
Contact List
Stephen Holman
contact affiliationUniversity of Liverpool
contact emailstephen.holman@liverpool.ac.uk
dataset submitter
Professor Robert J. Beynon
contact affiliationUniversity of Liverpool
contact emailr.beynon@liv.ac.uk
lab head
Full Dataset Link List
PeptideAtlas dataset URI
PASSEL experiment URI
PASSEL transition group browser URI