Tandem mass tags: a novel quantification strategy for comparative analysis of complex protein mixtures by MS/MS.

By Andrew Thompson, Jürgen Schäfer, K. Kuhn, S. Kienle, J. Schwarz, G. Schmidt, T. Neumann, R. Johnstone, A. K. A. Mohammed, C. Hamon. Analytical Chemistry, 2003

2,343 citations recorded by the source corpus.

Subfields: Analytical Chemistry, Spectroscopy

View Paper: https://www.semanticscholar.org/paper/663c38a053775133b7b777f9e90072ab2a2a84d9

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Citations in the corpus

Integrated Proteogenomic Characterization of Clear Cell Renal Cell Carcinoma (2019, background): “Inherent benefits of isobaric tag approaches over LFQ for protein quantitation include decreasing peptide/protein quantification differences attributed to variation in instrument performance, reducing the number “missing values,” and facilitating integrated measurements of global protein and post-tr”
Data‐independent acquisition‐based SWATH‐MS for quantitative proteomics: a tutorial (2018, neutral): “A second popular strategy for large-scale quantitative proteomics relies on isobaric labelling, using, for example, tandem mass tags (TMT) (Thompson et al , 2003) or isobaric tags for relative and absolute quantitation (iTRAQ) (Unwin et al , 2005).”
The MaxQuant computational platform for mass spectrometry-based shotgun proteomics (2016, methodology): “19| Set the type of analysis according to the quantification strategy in the ‘Type’ page ( Fig.”
A Guided Tour of the Trans-Proteomic Pipeline (2010, methodology): “Another popular technique is isobaric labeling such as iTRAQ [33] and TMT [34], where peptides in up to eight samples can be labeled with N-terminal isobaric labels, each with a different fragment ion peak near 100 m / z .”
Selected reaction monitoring for quantitative proteomics: a tutorial (2008, methodology): “The main exception to this rule are isobaric reagents like TMT (Thompson et al, 2003) or iTRAQ (Ross et al, 2004) where all peptides share the same reporter ions and are only distinguished by the precursor mass.”
Proteomics by mass spectrometry: approaches, advances, and applications. (2009, background): “Techniques such as ICAT (148), O18 labeling (149), and Hamon tandem mass tags (150) work best with flexible and accessible peptides.”
Online Parallel Accumulation–Serial Fragmentation (PASEF) with a Novel Trapped Ion Mobility Mass Spectrometer (2018, neutral): “methods, for example isobaric labeling with TMT (52), iTRAQ (53) or EASI-tag (54).”
Ultrasensitive proteome analysis using paramagnetic bead technology (2014, neutral): “The two most frequently applied chemical labeling approaches, reductive dimethylation (Boersema et al , 2009) and isobaric mass tagging (Thompson et al , 2003; Ross et al , 2004), are based on amine-reactive chemistry and thus have specific buffer and solution composition requirements.”
jPOSTrepo: an international standard data repository for proteomes (2016, methodology): “For isobaric labelling experiments, such as iTRAQ (16) and Tandem Mass Tag (17), multiple samples labeled by isobaric tags are measured at the same time.”
Multiplexed Protein Quantitation in Saccharomyces cerevisiae Using Amine-reactive Isobaric Tagging Reagents*S (2004, neutral): “Strategies have been described that employ isobaric peptide derivatives (13).”
SCoPE-MS: mass spectrometry of single mammalian cells quantifies proteome heterogeneity during cell differentiation (2017, methodology): “Even more crucial to our application, TMT allows quantifying the level of each TMT-labeled peptide in each sample while identifying its sequence from the total peptide amount pooled across all samples [32, 33].”