Evidence map›Paper›PMID 27259237›Full record

ArticleOncotarget2016

In-depth mapping of the mouse brain N-glycoproteome reveals widespread N-glycosylation of diverse brain proteins.

Pan Fang, Xin-Jian Wang, Yu Xue, Ming-Qi Liu, Wen-Feng Zeng, Yang Zhang, Lei Zhang, Xing Gao, Guo-Quan Yan, Jun Yao and 2 more

Open access · diamondAbstract read
In one paragraph

Article in Oncotarget, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
2.3field-weighted citation impact, top 12% of its field
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

21 citing papers in PubMed, 32 citations in OpenAlex.

  1. Article
  2. bioRxiv : the preprint server for biology · 2024
    Article
  3. Axonal pathfinding during the development of the nervous system.Annals of the Child Neurology Society · 2023
    Review
  4. Article
  5. Review
  6. Article
  7. Glycosylation in Axonal Guidance.International journal of molecular sciences · 2021
    Review
  8. Review
  9. Review
  10. Review
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Review
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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

12 authors at 2 institutions in 1 country.

Pan FangMinhang Hospital and Institutes of Biomedical Sciences, Fudan University, Shanghai, China.
Xin-Jian WangState Key Laboratory of Medical Neurobiology, Institutes of Brain Science, and Collaborative Innovation Center for Brain Science, Fudan University, Shanghai, China.
Yu XueDepartment of Chemistry, Fudan University, Shanghai, China.
Ming-Qi LiuMinhang Hospital and Institutes of Biomedical Sciences, Fudan University, Shanghai, China.
Wen-Feng ZengKey Laboratory of Intelligent Information Processing of Chinese Academy of Sciences (CAS), Institute of Computing Technology, CAS, Beijing, China.
Yang ZhangMinhang Hospital and Institutes of Biomedical Sciences, Fudan University, Shanghai, China.
Lei ZhangMinhang Hospital and Institutes of Biomedical Sciences, Fudan University, Shanghai, China.
Xing GaoMinhang Hospital and Institutes of Biomedical Sciences, Fudan University, Shanghai, China.
Guo-Quan YanDepartment of Chemistry, Fudan University, Shanghai, China.
Jun YaoMinhang Hospital and Institutes of Biomedical Sciences, Fudan University, Shanghai, China.
Hua-Li ShenMinhang Hospital and Institutes of Biomedical Sciences, Fudan University, Shanghai, China.
Peng-Yuan YangMinhang Hospital and Institutes of Biomedical Sciences, Fudan University, Shanghai, China.
Fudan University · CNInstitute of Computing Technology · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

N-glycosylation is one of the most prominent and abundant posttranslational modifications of proteins. It is estimated that over 50% of mammalian proteins undergo glycosylation. However, the analysis of N-glycoproteins has been limited by the available analytical technology. In this study, we comprehensively mapped the N-glycosylation sites in the mouse brain proteome by combining complementary methods, which included seven protease treatments, four enrichment techniques and two fractionation strategies. Altogether, 13492 N-glycopeptides containing 8386 N-glycosylation sites on 3982 proteins were identified. After evaluating the performance of the above methods, we proposed a simple and efficient workflow for large-scale N-glycosylation site mapping. The optimized workflow yielded 80% of the initially identified N-glycosylation sites with considerably less effort. Analysis of the identified N-glycoproteins revealed that many of the mouse brain proteins are N-glycosylated, including those proteins in critical pathways for nervous system development and neurological disease. Additionally, several important biomarkers of various diseases were found to be N-glycosylated. These data confirm that N-glycosylation is important in both physiological and pathological processes in the brain, and provide useful details about numerous N-glycosylation sites in brain proteins.

Indexed as

ProteomeAnimalsBiomarkersBrainComputational BiologyGlycoproteinsGlycosylationHydrogen-Ion ConcentrationMaleMiceMice, Inbred C57BLProtein Processing, Post-TranslationalProteomicsTandem Mass SpectrometryBiomarkersGlycoproteinsProteomebrain physiological activitiesdisease biomarkermass spectrometrymouse brainN-glycoproteomics

Identifiers

PMID27259237
PMCPMC5122430
OpenAlexW2417586279

What OpenQuestion holds

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LicenceCC BY
Read underepoch 390

Registered trials

None linked

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.