中国科学院机构知识库网格
Chinese Academy of Sciences Institutional Repositories Grid
Endo-M Mediated Chemoenzymatic Approach Enables Reversible Glycopeptide Labeling for O-GlcNAcylation Analysis

文献类型:期刊论文

作者Chen, Yao2,3; Tang, Feng3,4; Qin, Hongqiang2,3; Yue, Xuyang2; Nie, Yongzhan1,5; Huang, Wei3,4; Ye, Mingliang2,3
刊名ANGEWANDTE CHEMIE-INTERNATIONAL EDITION
出版日期2022-03-30
页码9
ISSN号1433-7851
关键词Chemoenzymatic Labeling Glycopeptide Enrichment Glycoproteomics Hydrophilic Interaction Liquid Chromatography O-GlcNAcylation
DOI10.1002/anie.202117849
通讯作者Qin, Hongqiang(qinhq@dicp.ac.cn) ; Huang, Wei(huangwei@simm.ac.cn) ; Ye, Mingliang(mingliang@dicp.ac.cn)
英文摘要To selectively enrich O-linked beta-N-acetylglucosamine (O-GlcNAc) peptides in their original form from complex samples, we report the first reversible chemoenzymatic labeling approach for proteomic analysis. In this strategy, the O-GlcNAc moieties are ligated with long N-glycans using an Endo-M mutant, which enables the enrichment of the labeled glycopeptides by hydrophilic interaction liquid chromatography (HILIC). The attached glycans on the enriched glycopeptides are removed by wild-type Endo-M/S to restore the O-GlcNAc moiety. Compared with classic chemoenzymatic labeling, this approach enables the tag-free identification, and eliminates the interference of bulky tags in glycopeptide detection. This approach presents a unique avenue for the proteome-wide analysis of protein O-GlcNAcylation to promote its mechanism research.
WOS关键词BETA-N-ACETYLGLUCOSAMINE ; MODIFIED PROTEINS ; CROSS-TALK ; GLYCOSYLATION ; PHOSPHORYLATION ; TRANSCRIPTION ; DYNAMICS ; STRESS
资助项目National Natural Science Foundation of China[81730016] ; National Natural Science Foundation of China[21775146] ; National Natural Science Foundation of China[22034007] ; National Key Research and Development Program of China[2017YFA0505003] ; National Key Research and Development Program of China[2020YFE0202200] ; Innovation Program of Science and Research from the DICP, CAS[DICP I201919] ; Innovation Program of Science and Research from the DICP, CAS[DICPQIBEBT UN201802] ; Youth Innovation Promotion Association of CAS[2018212]
WOS研究方向Chemistry
语种英语
出版者WILEY-V C H VERLAG GMBH
WOS记录号WOS:000775116900001
源URL[http://119.78.100.183/handle/2S10ELR8/299960]  
专题中国科学院上海药物研究所
通讯作者Qin, Hongqiang; Huang, Wei; Ye, Mingliang
作者单位1.Fourth Mil Med Univ, Natl Clin Res Ctr Digest Dis, State Key Lab Canc Biol, Xian 710032, Peoples R China
2.Chinese Acad Sci, Dalian Inst Chem Phys, CAS Key Lab Separat Sci Analyt Chem, Dalian 116023, Peoples R China
3.Univ Chinese Acad Sci, Beijing 101408, Peoples R China
4.Chinese Acad Sci, CAS Ctr Excellence Mol Cell Sci, Ctr Biotherapeut Discovery Res, Shanghai Inst Mat Med,CAS Key Lab Receptor Res, Shanghai 201203, Peoples R China
5.Fourth Mil Med Univ, Xijing Hosp Digest Dis, Xian 710032, Peoples R China
推荐引用方式
GB/T 7714
Chen, Yao,Tang, Feng,Qin, Hongqiang,et al. Endo-M Mediated Chemoenzymatic Approach Enables Reversible Glycopeptide Labeling for O-GlcNAcylation Analysis[J]. ANGEWANDTE CHEMIE-INTERNATIONAL EDITION,2022:9.
APA Chen, Yao.,Tang, Feng.,Qin, Hongqiang.,Yue, Xuyang.,Nie, Yongzhan.,...&Ye, Mingliang.(2022).Endo-M Mediated Chemoenzymatic Approach Enables Reversible Glycopeptide Labeling for O-GlcNAcylation Analysis.ANGEWANDTE CHEMIE-INTERNATIONAL EDITION,9.
MLA Chen, Yao,et al."Endo-M Mediated Chemoenzymatic Approach Enables Reversible Glycopeptide Labeling for O-GlcNAcylation Analysis".ANGEWANDTE CHEMIE-INTERNATIONAL EDITION (2022):9.

入库方式: OAI收割

来源:上海药物研究所

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