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A large-scale targeted proteomics assay resource based on an in vitro human proteome
- Source :
- Nature Methods. 14:251-258
- Publication Year :
- 2016
- Publisher :
- Springer Science and Business Media LLC, 2016.
-
Abstract
- Targeted proteomics approaches are of value for deep and accurate quantification of protein abundance. Extending such methods to quantify large numbers of proteins requires the construction of predefined targeted assays. We developed a targeted proteomics platform-in vitro proteome-assisted multiple reaction monitoring (MRM) for protein absolute quantification (iMPAQT)-by using >18,000 human recombinant proteins, thus enabling protein absolute quantification on a genome-wide scale. Our platform comprises experimentally confirmed MRM assays of mass tag (mTRAQ)-labeled peptides to allow for rapid and straightforward measurement of the absolute abundance of predefined sets of proteins by mass spectrometry. We applied iMPAQT to delineate the quantitative metabolic landscape of normal and transformed human fibroblasts. Oncogenic transformation gave rise to relatively small but global changes in metabolic pathways resulting in aerobic glycolysis (Warburg effect) and increased rates of macromolecule synthesis. iMPAQT should facilitate quantitative biology studies based on protein abundance measurements.
- Subjects :
- Proteomics
0301 basic medicine
Proteome
Computational biology
Mass spectrometry
Biochemistry
Mass Spectrometry
law.invention
03 medical and health sciences
0302 clinical medicine
Peptide Library
law
Human proteome project
Humans
Molecular Biology
Cell Line, Transformed
Genome, Human
Chemistry
Selected reaction monitoring
Cell Biology
Fibroblasts
Warburg effect
Molecular biology
Recombinant Proteins
In vitro
Metabolic pathway
030104 developmental biology
Anaerobic glycolysis
030220 oncology & carcinogenesis
Recombinant DNA
Glycolysis
Biotechnology
Subjects
Details
- ISSN :
- 15487105 and 15487091
- Volume :
- 14
- Database :
- OpenAIRE
- Journal :
- Nature Methods
- Accession number :
- edsair.doi.dedup.....46731883ad1108e45c22b0af77b5bab9
- Full Text :
- https://doi.org/10.1038/nmeth.4116