PXD010563
PXD010563 is an original dataset announced via ProteomeXchange.
Dataset Summary
Title | UoL_turnover_SRM (Holman et al. 2016) |
Description | Protein 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. |
HostingRepository | PeptideAtlas |
AnnounceDate | 2018-07-25 |
AnnouncementXML | Submission_2018-07-25_10:11:16.xml |
DigitalObjectIdentifier | |
ReviewLevel | Peer-reviewed dataset |
DatasetOrigin | Original dataset |
RepositorySupport | Supported dataset by repository |
PrimarySubmitter | Stephen Holman |
SpeciesList | scientific name: Mus musculus; NCBI TaxID: 10090; |
ModificationList | S-carboxamidomethyl-L-cysteine; 6x(13)C labeled L-lysine |
Instrument | TSQ Vantage |
Dataset History
Revision | Datetime | Status | ChangeLog Entry |
---|---|---|---|
0 | 2018-07-25 10:08:47 | ID requested | |
⏵ 1 | 2018-07-25 10:11:17 | announced |
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 affiliation | University of Liverpool |
contact email | stephen.holman@liverpool.ac.uk |
dataset submitter | |
Professor Robert J. Beynon | |
contact affiliation | University of Liverpool |
contact email | r.beynon@liv.ac.uk |
lab head |
Full Dataset Link List
PeptideAtlas dataset URI |
PASSEL experiment URI |
PASSEL transition group browser URI |