Evidence map›Paper›PMID 33067390›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2020

Mapping glycan-mediated galectin-3 interactions by live cell proximity labeling.

Eugene Joeh, Timothy O'Leary, Weichao Li, Richard Hawkins, Jonathan R Hung, Christopher G Parker, Mia L Huang

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 48 papers.

0numbers the graph read from it
0cells of the map it votes in
48citing 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

48 citing papers in PubMed, 69 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Review
  5. Protein engineering: status report.Protein engineering, design & selection : PEDS · 2026
    Review
  6. Article
  7. Article
  8. Article
  9. Article
  10. Review
  11. Chimerolectins: Classification, structural architecture, and functional perspectives.Protein science : a publication of the Protein Society · 2025
    Review
  12. Article
  13. 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
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Article
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 1 institution in 1 country.

Eugene JoehDepartment of Molecular Medicine, The Scripps Research Institute, Jupiter, FL 33458.
Timothy O'LearyDepartment of Molecular Medicine, The Scripps Research Institute, Jupiter, FL 33458.
Weichao LiDepartment of Molecular Medicine, The Scripps Research Institute, Jupiter, FL 33458.
Richard HawkinsDepartment of Molecular Medicine, The Scripps Research Institute, Jupiter, FL 33458.
Jonathan R HungDepartment of Molecular Medicine, The Scripps Research Institute, Jupiter, FL 33458.
Christopher G ParkerDepartment of Chemistry, The Scripps Research Institute, Jupiter, FL 33458.ORCID 0000-0001-8509-9289
Mia L HuangDepartment of Molecular Medicine, The Scripps Research Institute, Jupiter, FL 33458; miahuang@scripps.edu.ORCID 0000-0001-9909-9554
Scripps Research Institute · US

Funding

Bridging the Glycome and Proteome with Chemical BiologyR35GM142462 · NIGMS · SCRIPPS RESEARCH INSTITUTE, THE · PI Mia L Huang · 2021 to 2026
$2.9M
Illuminating Galectin-3 Interactions to Disrupt Hepatic FibrosisR56DK126895 · NIDDK · SCRIPPS RESEARCH INSTITUTE, THE · PI HUANG, MIA L · 2021 to 2021
$490k
NIDDK NIH HHS R56 DK126895NIGMS NIH HHS R35 GM142462
6 · The paper itself

Abstract

Galectin-3 is a glycan-binding protein (GBP) that binds β-galactoside glycan structures to orchestrate a variety of important biological events, including the activation of hepatic stellate cells and regulation of immune responses. While the requisite glycan epitopes needed to bind galectin-3 have long been elucidated, the cellular glycoproteins that bear these glycan signatures remain unknown. Given the importance of the three-dimensional (3D) arrangement of glycans in dictating GBP interactions, strategies that allow the identification of GBP receptors in live cells, where the native glycan presentation and glycoprotein expression are preserved, have significant advantages over static and artificial systems. Here we describe the integration of a proximity labeling method and quantitative mass spectrometry to map the glycan and glycoprotein interactors for galectin-3 in live human hepatic stellate cells and peripheral blood mononuclear cells. Understanding the identity of the glycoproteins and defining the structures of the glycans will empower efforts to design and develop selective therapeutics to mitigate galectin-3-mediated biological events.

Indexed as

Cell Culture TechniquesGalectin 3GalectinsGlycoproteinsHumansLeukocytes, MononuclearPolysaccharidesProtein BindingProtein Interaction Domains and MotifsSignal TransductionGalectin 3GalectinsGlycoproteinsPolysaccharidesgalectinsglycanglycomicsproteomicsproximity labeling

Identifiers

PMID33067390
PMCPMC7959530
OpenAlexW3093011960

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.