Evidence map›Paper›PMID 29382172›Full record

ReviewInternational journal of molecular sciences2018

Dissecting the Structure-Activity Relationship of Galectin-Ligand Interactions.

Yi-Chen Chan, Hsien-Ya Lin, Zhijay Tu, Yen-Hsi Kuo, Shang-Te Danny Hsu, Chun-Hung Lin

Open access · goldAbstract readReview
In one paragraph

Review in International journal of molecular sciences, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers.

0numbers the graph read from it
0cells of the map it votes in
41citing papers in PubMed
3.2field-weighted citation impact, top 8% 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

41 citing papers in PubMed, 76 citations in OpenAlex.

  1. Review
  2. Review
  3. Journal of medicinal chemistry · 2025
    Article
  4. Review
  5. Article
  6. The Role of Glycans in Human Immunity-A Sweet Code.Molecules (Basel, Switzerland) · 2025
    Review
  7. Review
  8. Article
  9. Article
  10. Review
  11. Article
  12. Article
  13. Article
  14. Article
  15. Review
  16. Review
  17. Galectin-1 and Galectin-3 in B-Cell Precursor Acute Lymphoblastic Leukemia.International journal of molecular sciences · 2022
    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

6 authors at 3 institutions in 1 country.

Yi-Chen ChanInstitute of Biological Chemistry, Academia Sinica, No. 128, Academia Road Section 2, Nan-Kang, Taipei 11529, Taiwan. cyc1786@yahoo.com.
Hsien-Ya LinInstitute of Biological Chemistry, Academia Sinica, No. 128, Academia Road Section 2, Nan-Kang, Taipei 11529, Taiwan. pipis_lsy@hotmail.com.
Zhijay TuInstitute of Biological Chemistry, Academia Sinica, No. 128, Academia Road Section 2, Nan-Kang, Taipei 11529, Taiwan. s42304@yahoo.com.tw.ORCID 0000-0002-3531-9439
Yen-Hsi KuoInstitute of Biological Chemistry, Academia Sinica, No. 128, Academia Road Section 2, Nan-Kang, Taipei 11529, Taiwan. yenkuo1@gmail.com.
Shang-Te Danny HsuInstitute of Biological Chemistry, Academia Sinica, No. 128, Academia Road Section 2, Nan-Kang, Taipei 11529, Taiwan. sthsu@gate.sinica.edu.tw.ORCID 0000-0002-7231-0185
Chun-Hung LinInstitute of Biological Chemistry, Academia Sinica, No. 128, Academia Road Section 2, Nan-Kang, Taipei 11529, Taiwan. chunhung@gate.sinica.edu.tw.
Institute of Biological Chemistry, Academia Sinica · TWNational Taiwan University · TWNational Yang Ming Chiao Tung University · TW

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Galectins are β-galactoside-binding proteins. As carbohydrate-binding proteins, they participate in intracellular trafficking, cell adhesion, and cell-cell signaling. Accumulating evidence indicates that they play a pivotal role in numerous physiological and pathological activities, such as the regulation on cancer progression, inflammation, immune response, and bacterial and viral infections. Galectins have drawn much attention as targets for therapeutic interventions. Several molecules have been developed as galectin inhibitors. In particular, TD139, a thiodigalactoside derivative, is currently examined in clinical trials for the treatment of idiopathic pulmonary fibrosis. Herein, we provide an in-depth review on the development of galectin inhibitors, aiming at the dissection of the structure-activity relationship to demonstrate how inhibitors interact with galectin(s). We especially integrate the structural information established by X-ray crystallography with several biophysical methods to offer, not only in-depth understanding at the molecular level, but also insights to tackle the existing challenges.

Indexed as

Quantitative Structure-Activity RelationshipAnimalsBinding SitesGalectinsHumansMolecular Docking SimulationProtein BindingThiogalactosidesGalectinsthiodigalactosideThiogalactosidesbinding interactiongalectininhibitorisothermal titration calorimetryNMR (Nuclear Magnetic Resonance)thiodigalactosideX-ray crystallography

Identifiers

PMID29382172
PMCPMC5855614
OpenAlexW2788992770

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.