EASI-tag enables accurate multiplexed and interference-free MS2-based proteome quantification

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Standard

EASI-tag enables accurate multiplexed and interference-free MS2-based proteome quantification. / Virreira Winter, Sebastian; Meier, Florian; Wichmann, Christoph; Cox, Juergen; Mann, Matthias; Meissner, Felix.

I: Nature Methods, Bind 15, Nr. 7, 2018, s. 527-530.

Publikation: Bidrag til tidsskrift › Tidsskriftartikel › Forskning › fagfællebedømt

Harvard

Virreira Winter, S, Meier, F, Wichmann, C, Cox, J, Mann, M & Meissner, F 2018, 'EASI-tag enables accurate multiplexed and interference-free MS2-based proteome quantification', Nature Methods, bind 15, nr. 7, s. 527-530. https://doi.org/10.1038/s41592-018-0037-8

APA

Virreira Winter, S., Meier, F., Wichmann, C., Cox, J., Mann, M., & Meissner, F. (2018). EASI-tag enables accurate multiplexed and interference-free MS2-based proteome quantification. Nature Methods, 15(7), 527-530. https://doi.org/10.1038/s41592-018-0037-8

Vancouver

Virreira Winter S, Meier F, Wichmann C, Cox J, Mann M, Meissner F. EASI-tag enables accurate multiplexed and interference-free MS2-based proteome quantification. Nature Methods. 2018;15(7):527-530. https://doi.org/10.1038/s41592-018-0037-8

Author

Virreira Winter, Sebastian ; Meier, Florian ; Wichmann, Christoph ; Cox, Juergen ; Mann, Matthias ; Meissner, Felix. / EASI-tag enables accurate multiplexed and interference-free MS2-based proteome quantification. I: Nature Methods. 2018 ; Bind 15, Nr. 7. s. 527-530.

Bibtex

@article{7bd475c5c0564472a7ed89ca06fc8060,
title = "EASI-tag enables accurate multiplexed and interference-free MS2-based proteome quantification",
abstract = "We developed EASI-tag (easily abstractable sulfoxide-based isobaric-tag), a new type of amine-derivatizing and sulfoxide-containing isobaric labeling reagents for highly accurate quantitative proteomics analysis using mass spectrometry. We observed that EASI-tag labels dissociate at low collision energy and generate peptide-coupled, interference-free reporter ions with high yield. Efficient isolation of 12C precursors and quantification at the MS2 level allowed accurate determination of quantitative differences between up to six multiplexed samples.",
author = "{Virreira Winter}, Sebastian and Florian Meier and Christoph Wichmann and Juergen Cox and Matthias Mann and Felix Meissner",
year = "2018",
doi = "10.1038/s41592-018-0037-8",
language = "English",
volume = "15",
pages = "527--530",
journal = "Nature Methods",
issn = "1548-7091",
publisher = "nature publishing group",
number = "7",

}

RIS

TY - JOUR

T1 - EASI-tag enables accurate multiplexed and interference-free MS2-based proteome quantification

AU - Virreira Winter, Sebastian

AU - Meier, Florian

AU - Wichmann, Christoph

AU - Cox, Juergen

AU - Mann, Matthias

AU - Meissner, Felix

PY - 2018

Y1 - 2018

N2 - We developed EASI-tag (easily abstractable sulfoxide-based isobaric-tag), a new type of amine-derivatizing and sulfoxide-containing isobaric labeling reagents for highly accurate quantitative proteomics analysis using mass spectrometry. We observed that EASI-tag labels dissociate at low collision energy and generate peptide-coupled, interference-free reporter ions with high yield. Efficient isolation of 12C precursors and quantification at the MS2 level allowed accurate determination of quantitative differences between up to six multiplexed samples.

AB - We developed EASI-tag (easily abstractable sulfoxide-based isobaric-tag), a new type of amine-derivatizing and sulfoxide-containing isobaric labeling reagents for highly accurate quantitative proteomics analysis using mass spectrometry. We observed that EASI-tag labels dissociate at low collision energy and generate peptide-coupled, interference-free reporter ions with high yield. Efficient isolation of 12C precursors and quantification at the MS2 level allowed accurate determination of quantitative differences between up to six multiplexed samples.

U2 - 10.1038/s41592-018-0037-8

DO - 10.1038/s41592-018-0037-8

M3 - Journal article

C2 - 29915187

VL - 15

SP - 527

EP - 530

JO - Nature Methods

JF - Nature Methods

SN - 1548-7091

IS - 7

ER -

ID: 198266076