Absolute quantification of proteins and phosphoproteins from cell lysates by tandem MS

By S. Gerber, John Rush, Olaf Stemman, Marc Kirschner, Steven P. Gygi. Proceedings of the National Academy of Sciences of the United States of America, 2003

1,751 citations recorded by the source corpus.

Subfields: Molecular Biology, Spectroscopy

View Paper: https://www.semanticscholar.org/paper/ef78edec9e6a053c2b47805198edde105d222dd5

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Citations in the corpus

Proteomics by mass spectrometry: approaches, advances, and applications. (2009, background): “Absolute measurements of protein concentrations can be achieved with spiked synthetic peptides (171), artificial proteins derived from detected peptides, as in QconCAT (172), and SILAC (173).”
Quantitative Mass Spectrometric Multiple Reaction Monitoring Assays for Major Plasma Proteins* (2006, background): “In this case, a specific tryptic peptide can be selected as a stoichiometric representative of the protein from which it is cleaved and quantitated against a spiked internal standard (a synthetic stable isotope-labeled peptide (14)) to yield a measure of protein concentration.”
Protein biomarker discovery and validation: the long and uncertain path to clinical utility (2006, methodology): “Quantification of candidate proteins was subsequently accomplished by selecting tryptic 'signature' peptides based on the sequence of the target protein, synthesizing them in deuterated, 15 N- or 13 C-labeled form, adding them to the sample, trypsin-digesting the mixture and analyzing the resultan”
Options and considerations when selecting a quantitative proteomics strategy (2010, background): “Accurate quantification depends on the addition of isotope-labeled reference molecules to the sample”
Mapping protein post-translational modifications with mass spectrometry (2007, background): “Absolute phosphopeptide abundances are not commonly quantified, but can be measured using isotopic dilutio”
The biological impact of mass-spectrometry-based proteomics (2007, methodology): “Using other strategies such as accurate mass tagging and single-ion reaction monitoring of peptides can increase throughput and reduce sample demands, but they limit the analysis to peptides or proteins that are known to be present in a mixture and, therefore, preclude serendipitous discoverie”
Quantitative, Multiplexed Assays for Low Abundance Proteins in Plasma by Targeted Mass Spectrometry and Stable Isotope Dilution*S (2007, background): “Monitoring a single transition per peptide has been proposed as being sufficiently specific for peptide quantitation in complex mixtures (18).”
Computational prediction of proteotypic peptides for quantitative proteomics (2007, background): “Several mass spectrometry–based quantitative proteomics methods attempt to comprehensively identify and quantify constituent proteins in complex mixture”
Correlation of mRNA and protein in complex biological samples (2009, positive): “The absolute quantiﬁcation (AQUA) of proteins by mass spectrometry involves spiking known amounts of synthesized, stable isotope labeled peptides mimicking expected tryptic peptides into the digested protein sample [34].”