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N-GlycositeAtlas: a database resource for mass spectrometry-based human N-linked glycoprotein and glycosylation site mapping
被引:68
作者:

Sun, Shisheng
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Johns Hopkins Univ, Dept Pathol, Baltimore, MD 21287 USA
Northwest Univ, Coll Life Sci, Xian 710069, Shaanxi, Peoples R China Johns Hopkins Univ, Dept Pathol, Baltimore, MD 21287 USA

Hu, Yingwei
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Johns Hopkins Univ, Dept Pathol, Baltimore, MD 21287 USA Johns Hopkins Univ, Dept Pathol, Baltimore, MD 21287 USA

Ao, Minghui
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Johns Hopkins Univ, Dept Pathol, Baltimore, MD 21287 USA Johns Hopkins Univ, Dept Pathol, Baltimore, MD 21287 USA

Shah, Punit
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Johns Hopkins Univ, Dept Pathol, Baltimore, MD 21287 USA Johns Hopkins Univ, Dept Pathol, Baltimore, MD 21287 USA

Chen, Jing
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Johns Hopkins Univ, Dept Pathol, Baltimore, MD 21287 USA Johns Hopkins Univ, Dept Pathol, Baltimore, MD 21287 USA

Yang, Weiming
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Johns Hopkins Univ, Dept Pathol, Baltimore, MD 21287 USA Johns Hopkins Univ, Dept Pathol, Baltimore, MD 21287 USA

Jia, Xingwang
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Johns Hopkins Univ, Dept Pathol, Baltimore, MD 21287 USA Johns Hopkins Univ, Dept Pathol, Baltimore, MD 21287 USA

Tian, Yuan
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Johns Hopkins Univ, Dept Pathol, Baltimore, MD 21287 USA Johns Hopkins Univ, Dept Pathol, Baltimore, MD 21287 USA

Thomas, Stefani
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Johns Hopkins Univ, Dept Pathol, Baltimore, MD 21287 USA Johns Hopkins Univ, Dept Pathol, Baltimore, MD 21287 USA

Zhang, Hui
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Johns Hopkins Univ, Dept Pathol, Baltimore, MD 21287 USA Johns Hopkins Univ, Dept Pathol, Baltimore, MD 21287 USA
机构:
[1] Johns Hopkins Univ, Dept Pathol, Baltimore, MD 21287 USA
[2] Northwest Univ, Coll Life Sci, Xian 710069, Shaanxi, Peoples R China
基金:
美国国家卫生研究院;
中国国家自然科学基金;
关键词:
HYDROPHILIC INTERACTION CHROMATOGRAPHY;
HIGHLY SPECIFIC ENRICHMENT;
SOLID-PHASE EXTRACTION;
INTERACTION LIQUID-CHROMATOGRAPHY;
LECTIN AFFINITY-CHROMATOGRAPHY;
GLYCOPEPTIDE CAPTURE APPROACH;
LARGE-SCALE IDENTIFICATION;
CELL-SURFACE;
HYDRAZIDE CHEMISTRY;
HUMAN PLASMA;
D O I:
10.1186/s12014-019-9254-0
中图分类号:
Q5 [生物化学];
学科分类号:
071010 ;
081704 ;
摘要:
Background N-linked glycoprotein is a highly interesting class of proteins for clinical and biological research. The large-scale characterization of N-linked glycoproteins accomplished by mass spectrometry-based glycoproteomics has provided valuable insights into the interdependence of glycoprotein structure and protein function. However, these studies focused mainly on the analysis of specific sample type, and lack the integration of glycoproteomic data from different tissues, body fluids or cell types. Methods In this study, we collected the human glycosite-containing peptides identified through their de-glycosylated forms by mass spectrometry from over 100 publications and unpublished datasets generated from our laboratory. A database resource termed N-GlycositeAtlas was created and further used for the distribution analyses of glycoproteins among different human cells, tissues and body fluids. Finally, a web interface of N-GlycositeAtlas was created to maximize the utility and value of the database. Results The N-GlycositeAtlas database contains more than 30,000 glycosite-containing peptides (representing > 14,000 N-glycosylation sites) from more than 7200 N-glycoproteins from different biological sources including human-derived tissues, body fluids and cell lines from over 100 studies. Conclusions The entire human N-glycoproteome database as well as 22 sub-databases associated with individual tissues or body fluids can be downloaded from the N-GlycositeAtlas website at http://nglycositeatlas.biomarkercenter.org.
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Chinese Acad Sci, Dalian Inst Chem Phys, Natl Chromatog R&A Ctr, Key Lab Separat Sci Analyt Chem, Dalian 116023, Peoples R China Univ Ottawa, Fac Med, Dept Biochem Microbiol & Immunol, Ottawa Inst Syst Biol, Ottawa, ON K1H 8M5, Canada

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