中国科学院机构知识库网格
Chinese Academy of Sciences Institutional Repositories Grid
Click-iG: Simultaneous Enrichment and Profiling of Intact N-linked, O-GalNAc, and O-GlcNAcylated Glycopeptides

文献类型:期刊论文

作者Liu, Jialin1,2,5,6; Cheng, Bo5,6; Fan, Xinqi5,6; Zhou, Xinyue5,6; Wang, Jiankun5,6; Zhou, Wen5,6; Li, Hengyu5,6; Zeng, Wenfeng3,4; Yang, Pengyuan1,2; Chen, Xing5,6
刊名ANGEWANDTE CHEMIE-INTERNATIONAL EDITION
出版日期2023-07-25
页码12
ISSN号1433-7851
关键词Glycoproteomics Glycosylation Intact Glycosites Metabolic Labeling Unnatural Glycans
DOI10.1002/anie.202303410
英文摘要Proteins are ubiquitously modified with glycans of varied chemical structures through distinct glycosidic linkages, making the landscape of protein glycosylation challenging to map. Profiling of intact glycopeptides with mass spectrometry (MS) has recently emerged as a powerful tool for revealing matched information of the glycosylation sites and attached glycans (i.e., intact glycosites), but is largely limited to individual glycosylation types. Herein, we describe Click-iG, which integrates metabolic labeling of glycans with clickable unnatural sugars, an optimized MS method, and a tailored version of pGlyco3 software to enable simultaneous enrichment and profiling of three types of intact glycopeptides: N-linked, mucin-type O-linked, and O-GlcNAcylated glycopeptides. We demonstrate the utility of Click-iG by the identification of thousands of intact glycosites in cell lines and living mice. From the mouse lung, heart, and spleen, a total of 2053 intact N-glycosites, 262 intact O-GalNAc glycosites, and 1947 O-GlcNAcylation sites were identified. Click-iG-enabled comprehensive coverage of the protein glycosylation landscape lays the foundation for interrogating crosstalk between different glycosylation pathways.
资助项目National Natural Science Foundation of China[92153301] ; National Natural Science Foundation of China[2225000285] ; National Natural Science Foundation of China[22037001] ; National Key Ramp;D Program of China[2018YFA0507600]
WOS研究方向Chemistry
语种英语
出版者WILEY-V C H VERLAG GMBH
WOS记录号WOS:001035289900001
源URL[http://119.78.100.204/handle/2XEOYT63/21279]  
专题中国科学院计算技术研究所期刊论文_英文
通讯作者Chen, Xing
作者单位1.Fudan Univ, Inst Biomed Sci, Shanghai 200433, Peoples R China
2.Fudan Univ, Dept Chem, Shanghai 200433, Peoples R China
3.Chinese Acad Sci, Key Lab Intelligent Informat Proc, Beijing 100190, Peoples R China
4.Chinese Acad Sci, Inst Comp Technol, Beijing 100190, Peoples R China
5.Peking Univ, Coll Chem & Mol Engn, Peking Tsinghua Ctr Life Sci, Synthet & Funct Biomol Ctr,Beijing Natl Lab Mol Sc, Beijing 100871, Peoples R China
6.Peking Univ, Key Lab Bioorgan Chem & Mol Engn, Minist Educ, Beijing 100871, Peoples R China
推荐引用方式
GB/T 7714
Liu, Jialin,Cheng, Bo,Fan, Xinqi,et al. Click-iG: Simultaneous Enrichment and Profiling of Intact N-linked, O-GalNAc, and O-GlcNAcylated Glycopeptides[J]. ANGEWANDTE CHEMIE-INTERNATIONAL EDITION,2023:12.
APA Liu, Jialin.,Cheng, Bo.,Fan, Xinqi.,Zhou, Xinyue.,Wang, Jiankun.,...&Chen, Xing.(2023).Click-iG: Simultaneous Enrichment and Profiling of Intact N-linked, O-GalNAc, and O-GlcNAcylated Glycopeptides.ANGEWANDTE CHEMIE-INTERNATIONAL EDITION,12.
MLA Liu, Jialin,et al."Click-iG: Simultaneous Enrichment and Profiling of Intact N-linked, O-GalNAc, and O-GlcNAcylated Glycopeptides".ANGEWANDTE CHEMIE-INTERNATIONAL EDITION (2023):12.

入库方式: OAI收割

来源:计算技术研究所

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