Evidence map›Paper›PMID 33581334›Full record

ArticleGenomics, proteomics & bioinformatics2021

OGP: A Repository of Experimentally Characterized O-glycoproteins to Facilitate Studies on O-glycosylation.

Jiangming Huang, Mengxi Wu, Yang Zhang, Siyuan Kong, Mingqi Liu, Biyun Jiang, Pengyuan Yang, Weiqian Cao

Abstract read
In one paragraph

Article in Genomics, proteomics & bioinformatics, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing 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

12 citing papers in PubMed.

  1. Article
  2. GalNAc-T13 maintains neurite architecture and memory retention via O-GalNAc glycosylation of seizure protein 6.Proceedings of the National Academy of Sciences of the United States of America · 2026
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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

8 authors.

Jiangming HuangDepartment of Chemistry and Institutes of Biomedical Sciences, Fudan University, Shanghai 200032, China; The Fifth People's Hospital, Fudan University, and the Shanghai Key Laboratory of Medical Epigenetics, the International Co-laboratory of Medical Epigenetics and Metabolism, Ministry of Science and Technology, Fudan University, Shanghai 200032, China.
Mengxi WuDepartment of Chemistry and Institutes of Biomedical Sciences, Fudan University, Shanghai 200032, China; The Fifth People's Hospital, Fudan University, and the Shanghai Key Laboratory of Medical Epigenetics, the International Co-laboratory of Medical Epigenetics and Metabolism, Ministry of Science and Technology, Fudan University, Shanghai 200032, China.
Yang ZhangDepartment of Chemistry and Institutes of Biomedical Sciences, Fudan University, Shanghai 200032, China; The Fifth People's Hospital, Fudan University, and the Shanghai Key Laboratory of Medical Epigenetics, the International Co-laboratory of Medical Epigenetics and Metabolism, Ministry of Science and Technology, Fudan University, Shanghai 200032, China.
Siyuan KongDepartment of Chemistry and Institutes of Biomedical Sciences, Fudan University, Shanghai 200032, China.
Mingqi LiuDepartment of Chemistry and Institutes of Biomedical Sciences, Fudan University, Shanghai 200032, China.
Biyun JiangDepartment of Chemistry and Institutes of Biomedical Sciences, Fudan University, Shanghai 200032, China; The Fifth People's Hospital, Fudan University, and the Shanghai Key Laboratory of Medical Epigenetics, the International Co-laboratory of Medical Epigenetics and Metabolism, Ministry of Science and Technology, Fudan University, Shanghai 200032, China.
Pengyuan YangDepartment of Chemistry and Institutes of Biomedical Sciences, Fudan University, Shanghai 200032, China; The Fifth People's Hospital, Fudan University, and the Shanghai Key Laboratory of Medical Epigenetics, the International Co-laboratory of Medical Epigenetics and Metabolism, Ministry of Science and Technology, Fudan University, Shanghai 200032, China; NHC Key Laboratory of Glycoconjugates Research (Fudan University), Shanghai 200032, China. Electronic address: pyyang@fudan.edu.cn.
Weiqian CaoDepartment of Chemistry and Institutes of Biomedical Sciences, Fudan University, Shanghai 200032, China; The Fifth People's Hospital, Fudan University, and the Shanghai Key Laboratory of Medical Epigenetics, the International Co-laboratory of Medical Epigenetics and Metabolism, Ministry of Science and Technology, Fudan University, Shanghai 200032, China; NHC Key Laboratory of Glycoconjugates Research (Fudan University), Shanghai 200032, China. Electronic address: wqcao@fudan.edu.cn.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Numerous studies on cancers, biopharmaceuticals, and clinical trials have necessitated comprehensive and precise analysis of protein O-glycosylation. However, the lack of updated and convenient databases deters the storage of and reference to emerging O-glycoprotein data. To resolve this issue, an O-glycoprotein repository named OGP was established in this work. It was constructed with a collection of O-glycoprotein data from different sources. OGP contains 9354 O-glycosylation sites and 11,633 site-specific O-glycans mapping to 2133 O-glycoproteins, and it is the largest O-glycoprotein repository thus far. Based on the recorded O-glycosylation sites, an O-glycosylation site prediction tool was developed. Moreover, an OGP-based website is already available (https://www.oglyp.org/). The website comprises four specially designed and user-friendly modules: statistical analysis, database search, site prediction, and data submission. The first version of OGP repository and the website allow users to obtain various O-glycoprotein-related information, such as protein accession Nos., O-glycosylation sites, O-glycopeptide sequences, site-specific O-glycan structures, experimental methods, and potential O-glycosylation sites. O-glycosylation data mining can be performed efficiently on this website, which will greatly facilitate related studies. In addition, the database is accessible from OGP website (https://www.oglyp.org/download.php).

Indexed as

GlycoproteinsDatabases, ProteinGlycosylationGlycoproteinsData miningO-glycoprotein related websiteO-glycoprotein repositoryO-glycosylationSite prediction

Identifiers

PMID33581334
PMCPMC9039567

What OpenQuestion holds

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LicenceCC BY
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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.