Glyco-DIA: a method for quantitative O-glycoproteomics with in silico-boosted glycopeptide libraries

Research output: Contribution to journal › Journal article › Research › peer-review

Standard

Glyco-DIA : a method for quantitative O-glycoproteomics with in silico-boosted glycopeptide libraries. / Ye, Zilu; Mao, Yang; Clausen, Henrik; Vakhrushev, Sergey Y.

In: Nature Methods, Vol. 16, No. 9, 2019, p. 902-910.

Research output: Contribution to journal › Journal article › Research › peer-review

Harvard

Ye, Z, Mao, Y, Clausen, H & Vakhrushev, SY 2019, 'Glyco-DIA: a method for quantitative O-glycoproteomics with in silico-boosted glycopeptide libraries', Nature Methods, vol. 16, no. 9, pp. 902-910. https://doi.org/10.1038/s41592-019-0504-x

APA

Ye, Z., Mao, Y., Clausen, H., & Vakhrushev, S. Y. (2019). Glyco-DIA: a method for quantitative O-glycoproteomics with in silico-boosted glycopeptide libraries. Nature Methods, 16(9), 902-910. https://doi.org/10.1038/s41592-019-0504-x

Vancouver

Ye Z, Mao Y, Clausen H, Vakhrushev SY. Glyco-DIA: a method for quantitative O-glycoproteomics with in silico-boosted glycopeptide libraries. Nature Methods. 2019;16(9):902-910. https://doi.org/10.1038/s41592-019-0504-x

Author

Ye, Zilu ; Mao, Yang ; Clausen, Henrik ; Vakhrushev, Sergey Y. / Glyco-DIA : a method for quantitative O-glycoproteomics with in silico-boosted glycopeptide libraries. In: Nature Methods. 2019 ; Vol. 16, No. 9. pp. 902-910.

Bibtex

@article{1e92f8630b3049d48209969498661e39,
title = "Glyco-DIA: a method for quantitative O-glycoproteomics with in silico-boosted glycopeptide libraries",
abstract = "We report a liquid chromatography coupled to tandem mass spectrometry O-glycoproteomics strategy using data-independent acquisition (DIA) mode for direct analysis of O-glycoproteins. This approach enables characterization of glycopeptides and structures of O-glycans on a proteome-wide scale with quantification of stoichiometries (though it does not allow for direct unambiguous glycosite identification). The method relies on a spectral library of O-glycopeptides; the Glyco-DIA library contains sublibraries obtained from human cell lines and human serum, and it currently covers 2,076 O-glycoproteins (11,452 unique glycopeptide sequences) and the 5 most common core1 O-glycan structures. Applying the Glyco-DIA library to human serum without enrichment for glycopeptides enabled us to identify and quantify 269 distinct glycopeptide sequences bearing up to 5 different core1 O-glycans from 159 glycoproteins in a SingleShot analysis.",
author = "Zilu Ye and Yang Mao and Henrik Clausen and Vakhrushev, {Sergey Y}",
year = "2019",
doi = "10.1038/s41592-019-0504-x",
language = "English",
volume = "16",
pages = "902--910",
journal = "Nature Methods",
issn = "1548-7091",
publisher = "nature publishing group",
number = "9",

}

RIS

TY - JOUR

T1 - Glyco-DIA

T2 - a method for quantitative O-glycoproteomics with in silico-boosted glycopeptide libraries

AU - Ye, Zilu

AU - Mao, Yang

AU - Clausen, Henrik

AU - Vakhrushev, Sergey Y

PY - 2019

Y1 - 2019

N2 - We report a liquid chromatography coupled to tandem mass spectrometry O-glycoproteomics strategy using data-independent acquisition (DIA) mode for direct analysis of O-glycoproteins. This approach enables characterization of glycopeptides and structures of O-glycans on a proteome-wide scale with quantification of stoichiometries (though it does not allow for direct unambiguous glycosite identification). The method relies on a spectral library of O-glycopeptides; the Glyco-DIA library contains sublibraries obtained from human cell lines and human serum, and it currently covers 2,076 O-glycoproteins (11,452 unique glycopeptide sequences) and the 5 most common core1 O-glycan structures. Applying the Glyco-DIA library to human serum without enrichment for glycopeptides enabled us to identify and quantify 269 distinct glycopeptide sequences bearing up to 5 different core1 O-glycans from 159 glycoproteins in a SingleShot analysis.

AB - We report a liquid chromatography coupled to tandem mass spectrometry O-glycoproteomics strategy using data-independent acquisition (DIA) mode for direct analysis of O-glycoproteins. This approach enables characterization of glycopeptides and structures of O-glycans on a proteome-wide scale with quantification of stoichiometries (though it does not allow for direct unambiguous glycosite identification). The method relies on a spectral library of O-glycopeptides; the Glyco-DIA library contains sublibraries obtained from human cell lines and human serum, and it currently covers 2,076 O-glycoproteins (11,452 unique glycopeptide sequences) and the 5 most common core1 O-glycan structures. Applying the Glyco-DIA library to human serum without enrichment for glycopeptides enabled us to identify and quantify 269 distinct glycopeptide sequences bearing up to 5 different core1 O-glycans from 159 glycoproteins in a SingleShot analysis.

U2 - 10.1038/s41592-019-0504-x

DO - 10.1038/s41592-019-0504-x

M3 - Journal article

C2 - 31384044

VL - 16

SP - 902

EP - 910

JO - Nature Methods

JF - Nature Methods

SN - 1548-7091

IS - 9

ER -

ID: 228734179