Evidence map›Paper›PMID 29531238›Full record

ArticleScientific reports2018

Loss and gain of N-linked glycosylation sequons due to single-nucleotide variation in cancer.

Yu Fan, Yu Hu, Cheng Yan, Radoslav Goldman, Yang Pan, Raja Mazumder, Hayley M Dingerdissen

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing papers in PubMed
1.2field-weighted citation impact, top 21% 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

10 citing papers in PubMed, 23 citations in OpenAlex.

  1. Revealing the Biological Effect of theJournal of the American Chemical Society · 2026
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  10. Oligosaccharyltransferase: A Gatekeeper of Health and Tumor Progression.International journal of molecular sciences · 2019
    Review
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

7 authors at 2 institutions in 1 country.

Yu FanThe Department of Biochemistry & Molecular Medicine, The George Washington University Medical Center, Washington, DC, 20037, United States of America.
Yu HuThe Department of Biochemistry & Molecular Medicine, The George Washington University Medical Center, Washington, DC, 20037, United States of America.
Cheng YanThe Department of Biochemistry & Molecular Medicine, The George Washington University Medical Center, Washington, DC, 20037, United States of America.
Radoslav GoldmanDepartment of Oncology, Georgetown University, Washington, DC, 20057, United States of America.
Yang PanThe Department of Biochemistry & Molecular Medicine, The George Washington University Medical Center, Washington, DC, 20037, United States of America.
Raja MazumderThe Department of Biochemistry & Molecular Medicine, The George Washington University Medical Center, Washington, DC, 20037, United States of America. mazumder@gwu.edu.
Hayley M DingerdissenThe Department of Biochemistry & Molecular Medicine, The George Washington University Medical Center, Washington, DC, 20037, United States of America. hmhamilt@gwmail.gwu.edu.ORCID 0000-0002-5323-2927
George Washington University · USGeorgetown University · US

Funding

Glycans in Hepatocellular CarcinomaR01CA135069 · NCI · GEORGETOWN UNIVERSITY · PI GOLDMAN, RADOSLAV · 2009 to 2019
$4.1M
Alliance of Glycobiologists for Detection of CancerU01CA168926 · NCI · GEORGETOWN UNIVERSITY · PI GOLDMAN, RADOSLAV · 2012 to 2016
$2.0M
NCI NIH HHS R01 CA135069NCI NIH HHS U01 CA168926
6 · The paper itself

Abstract

Despite availability of sequence site-specific information resulting from years of sequencing and sequence feature curation, there have been few efforts to integrate and annotate this information. In this study, we update the number of human N-linked glycosylation sequons (NLGs), and we investigate cancer-relatedness of glycosylation-impacting somatic nonsynonymous single-nucleotide variation (nsSNV) by mapping human NLGs to cancer variation data and reporting the expected loss or gain of glycosylation sequon. We find 75.8% of all human proteins have at least one NLG for a total of 59,341 unique NLGs (includes predicted and experimentally validated). Only 27.4% of all NLGs are experimentally validated sites on 4,412 glycoproteins. With respect to cancer, 8,895 somatic-only nsSNVs abolish NLGs in 5,204 proteins and 12,939 somatic-only nsSNVs create NLGs in 7,356 proteins in cancer samples. nsSNVs causing loss of 24 NLGs on 23 glycoproteins and nsSNVs creating 41 NLGs on 40 glycoproteins are identified in three or more cancers. Of all identified cancer somatic variants causing potential loss or gain of glycosylation, only 36 have previously known disease associations. Although this work is computational, it builds on existing genomics and glycobiology research to promote identification and rank potential cancer nsSNV biomarkers for experimental validation.

Indexed as

Polymorphism, Single NucleotideGenome, HumanGenomicsGlycoproteinsGlycosylationHumansNeoplasmsProteomeGlycoproteinsProteome

Identifiers

PMID29531238
PMCPMC5847511
OpenAlexW2800341279

What OpenQuestion holds

Textmetadata
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.