Evidence map›Paper›PMID 27282921›Full record

ArticleJournal of proteomics2016

Improvement of core-fucosylated glycoproteome coverage via alternating HCD and ETD fragmentation.

Cheng Ma, Jingyao Qu, Xu Li, Xinyuan Zhao, Lei Li, Cong Xiao, Garrett Edmunds, Ebtesam Gashash, Jing Song, Peng George Wang

Abstract read
In one paragraph

Article in Journal of proteomics, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

11 citing papers in PubMed.

  1. Review
  2. High-throughput site-specificNational science review · 2023
    Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Precision Mapping of O-LinkedJournal of the American Chemical Society · 2020
    Article
  8. Article
  9. Article
  10. Article
  11. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

10 authors.

Cheng MaDepartment of Chemistry, Center for Diagnostics & Therapeutics, Georgia State University, Atlanta, GA 30303, United States. Electronic address: cma@gsu.edu.
Jingyao QuDepartment of Chemistry, Center for Diagnostics & Therapeutics, Georgia State University, Atlanta, GA 30303, United States.
Xu LiDepartment of Chemistry, Center for Diagnostics & Therapeutics, Georgia State University, Atlanta, GA 30303, United States.
Xinyuan ZhaoNational Institute of Biological Sciences, Beijing 102206, People's Republic of China.
Lei LiDepartment of Chemistry, Center for Diagnostics & Therapeutics, Georgia State University, Atlanta, GA 30303, United States.
Cong XiaoDepartment of Chemistry, Center for Diagnostics & Therapeutics, Georgia State University, Atlanta, GA 30303, United States.
Garrett EdmundsDepartment of Chemistry, Center for Diagnostics & Therapeutics, Georgia State University, Atlanta, GA 30303, United States.
Ebtesam GashashDepartment of Chemistry, Center for Diagnostics & Therapeutics, Georgia State University, Atlanta, GA 30303, United States.
Jing SongDepartment of Chemistry, Center for Diagnostics & Therapeutics, Georgia State University, Atlanta, GA 30303, United States.
Peng George WangDepartment of Chemistry, Center for Diagnostics & Therapeutics, Georgia State University, Atlanta, GA 30303, United States. Electronic address: pwang11@gsu.edu.

Funding

Facile Synthesis of O-Glycans and O-GlycopeptidesU01GM116263 · NIGMS · GEORGIA STATE UNIVERSITY · PI LI, LEI · 2015 to 2018
$2.2M
NIGMS NIH HHS U01 GM116263
6 · The paper itself

Abstract

unlabelledCore-fucosylation (CF) plays important roles in regulating biological processes in eukaryotes. Alterations of CF-glycosites or CF-glycans in bodily fluids correlate with cancer development. Therefore, global research of protein core-fucosylation with an emphasis on proteomics can explain pathogenic and metastasis mechanisms and aid in the discovery of new potential biomarkers for early clinical diagnosis. In this study, a precise and high throughput method was established to identify CF-glycosites from human plasma. We found that alternating HCD and ETD fragmentation (AHEF) can provide a complementary method to discover CF-glycosites. A total of 407 CF-glycosites among 267 CF-glycoproteins were identified in a mixed sample made from six normal human plasma samples. Among the 407 CF-glycosites, 10 are without the N-X-S/T/C consensus motif, representing 2.5% of the total number identified. All identified CF-glycopeptide results from HCD and ETD fragmentation were filtered with neutral loss peaks and characteristic ions of GlcNAc from HCD spectra, which assured the credibility of the results. This study provides an effective method for CF-glycosites identification and a valuable biomarker reference for clinical research. BIOLOGICAL SIGNIFICANCE: CF-glycosytion plays an important role in regulating biological processes in eukaryotes. Alterations of the glycosites and attached CF-glycans are frequently observed in various types of cancers. Thus, it is crucial to develop a strategy for mapping human CF-glycosylation. Here, we developed a complementary method via alternating HCD and ETD fragmentation (AHEF) to analyze CF-glycoproteins. This strategy reveals an excellent complementarity of HCD and ETD in the analysis of CF-glycoproteins, and provides a valuable biomarker reference for clinical research.

Indexed as

Amino Acid MotifsBlood ProteinsConsensus SequenceFucoseGlycopeptidesGlycosylationHumansPeptide FragmentsProteomicsBlood ProteinsFucoseGlycopeptidesPeptide FragmentsCore-fucosylationETDHCDHuman plasma

Identifiers

PMID27282921
PMCPMC5953178

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Registered trials

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.