pGlyco 2.0 enables precision N-glycoproteomics with comprehensive quality control and one-step mass spectrometry for intact glycopeptide identification
Protein glycosylation is a heterogeneous post-translational modification that generates greater proteomic diversity that is difficult to analyze. Here the authors describe pGlyco 2.0, a workflow for the precise one step identification of intact N-glycopeptides at the proteome scale.
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Nature Portfolio
2017
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oai:doaj.org-article:396d0831a0fc493eb33a0808839d479d2021-12-02T17:01:18ZpGlyco 2.0 enables precision N-glycoproteomics with comprehensive quality control and one-step mass spectrometry for intact glycopeptide identification10.1038/s41467-017-00535-22041-1723https://doaj.org/article/396d0831a0fc493eb33a0808839d479d2017-09-01T00:00:00Zhttps://doi.org/10.1038/s41467-017-00535-2https://doaj.org/toc/2041-1723Protein glycosylation is a heterogeneous post-translational modification that generates greater proteomic diversity that is difficult to analyze. Here the authors describe pGlyco 2.0, a workflow for the precise one step identification of intact N-glycopeptides at the proteome scale.Ming-Qi LiuWen-Feng ZengPan FangWei-Qian CaoChao LiuGuo-Quan YanYang ZhangChao PengJian-Qiang WuXiao-Jin ZhangHui-Jun TuHao ChiRui-Xiang SunYong CaoMeng-Qiu DongBi-Yun JiangJiang-Ming HuangHua-Li ShenCatherine C. L. WongSi-Min HePeng-Yuan YangNature PortfolioarticleScienceQENNature Communications, Vol 8, Iss 1, Pp 1-14 (2017) |
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Science Q Ming-Qi Liu Wen-Feng Zeng Pan Fang Wei-Qian Cao Chao Liu Guo-Quan Yan Yang Zhang Chao Peng Jian-Qiang Wu Xiao-Jin Zhang Hui-Jun Tu Hao Chi Rui-Xiang Sun Yong Cao Meng-Qiu Dong Bi-Yun Jiang Jiang-Ming Huang Hua-Li Shen Catherine C. L. Wong Si-Min He Peng-Yuan Yang pGlyco 2.0 enables precision N-glycoproteomics with comprehensive quality control and one-step mass spectrometry for intact glycopeptide identification |
description |
Protein glycosylation is a heterogeneous post-translational modification that generates greater proteomic diversity that is difficult to analyze. Here the authors describe pGlyco 2.0, a workflow for the precise one step identification of intact N-glycopeptides at the proteome scale. |
format |
article |
author |
Ming-Qi Liu Wen-Feng Zeng Pan Fang Wei-Qian Cao Chao Liu Guo-Quan Yan Yang Zhang Chao Peng Jian-Qiang Wu Xiao-Jin Zhang Hui-Jun Tu Hao Chi Rui-Xiang Sun Yong Cao Meng-Qiu Dong Bi-Yun Jiang Jiang-Ming Huang Hua-Li Shen Catherine C. L. Wong Si-Min He Peng-Yuan Yang |
author_facet |
Ming-Qi Liu Wen-Feng Zeng Pan Fang Wei-Qian Cao Chao Liu Guo-Quan Yan Yang Zhang Chao Peng Jian-Qiang Wu Xiao-Jin Zhang Hui-Jun Tu Hao Chi Rui-Xiang Sun Yong Cao Meng-Qiu Dong Bi-Yun Jiang Jiang-Ming Huang Hua-Li Shen Catherine C. L. Wong Si-Min He Peng-Yuan Yang |
author_sort |
Ming-Qi Liu |
title |
pGlyco 2.0 enables precision N-glycoproteomics with comprehensive quality control and one-step mass spectrometry for intact glycopeptide identification |
title_short |
pGlyco 2.0 enables precision N-glycoproteomics with comprehensive quality control and one-step mass spectrometry for intact glycopeptide identification |
title_full |
pGlyco 2.0 enables precision N-glycoproteomics with comprehensive quality control and one-step mass spectrometry for intact glycopeptide identification |
title_fullStr |
pGlyco 2.0 enables precision N-glycoproteomics with comprehensive quality control and one-step mass spectrometry for intact glycopeptide identification |
title_full_unstemmed |
pGlyco 2.0 enables precision N-glycoproteomics with comprehensive quality control and one-step mass spectrometry for intact glycopeptide identification |
title_sort |
pglyco 2.0 enables precision n-glycoproteomics with comprehensive quality control and one-step mass spectrometry for intact glycopeptide identification |
publisher |
Nature Portfolio |
publishDate |
2017 |
url |
https://doaj.org/article/396d0831a0fc493eb33a0808839d479d |
work_keys_str_mv |
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