Evidence map›Paper›PMID 36525649›Full record

ArticleJournal of the American Chemical Society2022

Photoproximity Labeling of Sialylated Glycoproteins (GlycoMap) Reveals Sialylation-Dependent Regulation of Ion Transport.

Claudio F Meyer, Ciaran P Seath, Steve D Knutson, Wenyun Lu, Joshua D Rabinowitz, David W C MacMillan

Open access · greenAbstract read
In one paragraph

Article in Journal of the American Chemical Society, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
3.2field-weighted citation impact, top 7% 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

25 citing papers in PubMed, 40 citations in OpenAlex.

  1. Review
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  7. Article
  8. Metabolic control of glycosylation forms for establishing glycan-dependent protein interaction networks.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  9. Article
  10. Review
  11. Article
  12. Article
  13. Review
  14. Article
  15. Article
  16. Cancers · 2025
    Review
  17. Sialylation-immune-related lncRNAFrontiers in immunology · 2025
    Article
  18. Article
  19. Review
  20. 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

6 authors at 1 institution in 1 country.

Claudio F MeyerMerck Center for Catalysis at Princeton University, Princeton, New Jersey 08544, United States.
Ciaran P SeathMerck Center for Catalysis at Princeton University, Princeton, New Jersey 08544, United States.
Steve D KnutsonMerck Center for Catalysis at Princeton University, Princeton, New Jersey 08544, United States.ORCID 0000-0001-6822-464X
Wenyun LuDepartment of Chemistry, Princeton University, Princeton, New Jersey 08544, United States.ORCID 0000-0003-1787-2617
Joshua D RabinowitzDepartment of Chemistry, Princeton University, Princeton, New Jersey 08544, United States.ORCID 0000-0002-1247-4727
David W C MacMillanMerck Center for Catalysis at Princeton University, Princeton, New Jersey 08544, United States.ORCID 0000-0001-6447-0587
Princeton University · US

Funding

Photoredox Catalysis Applications in Organometallics and Chemical BiologyR35GM134897 · NIGMS · PRINCETON UNIVERSITY · PI David W MacMillan · 2020 to 2026
$6.3M
Revealing cancer metabolism via mass spectrometry and isotope tracersR50CA211437 · NCI · PRINCETON UNIVERSITY · PI Wenyun Lu · 2016 to 2026
$1.3M
High-Resolution Mapping of Subcellular RNA Dynamics Using Photocatalytic Proximity LabelingF32GM142206 · NIGMS · PRINCETON UNIVERSITY · PI KNUTSON, STEVEN DOUGLAS · 2021 to 2023
$202k
NCI NIH HHS R50 CA211437NIGMS NIH HHS F32 GM142206NIGMS NIH HHS R35 GM134897
6 · The paper itself

Abstract

Sialylation, the addition of sialic acid to glycans, is a crucial post-translational modification of proteins, contributing to neurodevelopment, oncogenesis, and immune response. In cancer, sialylation is dramatically upregulated. Yet, the functional biochemical consequences of sialylation remain mysterious. Here, we establish a μMap proximity labeling platform that utilizes metabolically inserted azidosialic acid to introduce iridium-based photocatalysts on sialylated cell-surface glycoproteins as a means to profile local microenvironments across the sialylated proteome. In comparative experiments between primary cervical cells and a cancerous cell line (HeLa), we identify key differences in both the global sialome and proximal proteins, including solute carrier proteins that regulate metabolite and ion transport. In particular, we show that cell-surface interactions between receptors trafficking ethanolamine and zinc are sialylation-dependent and impact intracellular metabolite levels. These results establish a μMap method for interrogating proteoglycan function and support a role for sialylated glycoproteins in regulating cell-surface transporters.

Indexed as

GlycoproteinsN-Acetylneuraminic AcidCell MembraneHumansIon TransportMembrane GlycoproteinsPolysaccharidesGlycoproteinsMembrane GlycoproteinsN-Acetylneuraminic AcidPolysaccharides

Identifiers

PMID36525649
PMCPMC10782853
OpenAlexW4311825265

What OpenQuestion holds

Textmetadata
LicenceTDM
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.