Evidence map›Paper›PMID 26015571›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2015

miRNA proxy approach reveals hidden functions of glycosylation.

Tomasz Kurcon, Zhongyin Liu, Anika V Paradkar, Christopher A Vaiana, Sujeethraj Koppolu, Praveen Agrawal, Lara K Mahal

Erratum issuedAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 30 papers.

0numbers the graph read from it
0cells of the map it votes in
30citing 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

30 citing papers in PubMed.

  1. Review
  2. Article
  3. The Critical Role of GALNTs-Regulated O-GalNAc Glycosylation in Cancer Malignancy.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2026
    Review
  4. Review
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Review
  11. Article
  12. Review
  13. Article
  14. Review
  15. Article
  16. Review
  17. Article
  18. Review
  19. Global view of human protein glycosylation pathways and functions.Nature reviews. Molecular cell biology · 2020
    Review
  20. Review
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

7 authors.

Tomasz KurconBiomedical Chemistry Institute, Department of Chemistry, New York University, New York, NY 10003.
Zhongyin LiuBiomedical Chemistry Institute, Department of Chemistry, New York University, New York, NY 10003.
Anika V ParadkarBiomedical Chemistry Institute, Department of Chemistry, New York University, New York, NY 10003.
Christopher A VaianaBiomedical Chemistry Institute, Department of Chemistry, New York University, New York, NY 10003.
Sujeethraj KoppoluBiomedical Chemistry Institute, Department of Chemistry, New York University, New York, NY 10003.
Praveen AgrawalBiomedical Chemistry Institute, Department of Chemistry, New York University, New York, NY 10003.
Lara K MahalBiomedical Chemistry Institute, Department of Chemistry, New York University, New York, NY 10003 lkmahal@nyu.edu.

Funding

NCI NIH HHS CA110602
6 · The paper itself

Abstract

Glycosylation, the most abundant posttranslational modification, holds an unprecedented capacity for altering biological function. Our ability to harness glycosylation as a means to control biological systems is hampered by our inability to pinpoint the specific glycans and corresponding biosynthetic enzymes underlying a biological process. Herein we identify glycosylation enzymes acting as regulatory elements within a pathway using microRNA (miRNA) as a proxy. Leveraging the target network of the miRNA-200 family (miR-200f), regulators of epithelial-to-mesenchymal transition (EMT), we pinpoint genes encoding multiple promesenchymal glycosylation enzymes (glycogenes). We focus on three enzymes, beta-1,3-glucosyltransferase (B3GLCT), beta-galactoside alpha-2,3-sialyltransferase 5 (ST3GAL5), and (alpha-N-acetyl-neuraminyl-2,3-beta-galactosyl-1,3)-N-acetylgalactosaminide alpha-2,6-sialyltransferase 5 (ST6GALNAC5), encoding glycans that are difficult to analyze by traditional methods. Silencing these glycogenes phenocopied the effect of miR-200f, inducing mesenchymal-to-epithelial transition. In addition, all three are up-regulated in TGF-β-induced EMT, suggesting tight integration within the EMT-signaling network. Our work indicates that miRNA can act as a relatively simple proxy to decrypt which glycogenes, including those encoding difficult-to-analyze structures (e.g., proteoglycans, glycolipids), are functionally important in a biological pathway, setting the stage for the rapid identification of glycosylation enzymes driving disease states.

Indexed as

Cell Line, TumorEpithelial-Mesenchymal TransitionGene SilencingGlycosylationHumansMicroRNAsReal-Time Polymerase Chain ReactionTransferasesMicroRNAsTransferasesepithelial to mesenchymal transitionglycan regulationglycomicsmiR-200TGF-beta

Identifiers

PMID26015571
PMCPMC4466752

What OpenQuestion holds

Textmetadata
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.