Evidence map›Paper›PMID 26543238›Full record

ArticleOncotarget2015

Design of a peptidic inhibitor that targets the dimer interface of a prototypic galectin.

Maria Claudia Vladoiu, Marilyne Labrie, Myriam Létourneau, Philippe Egesborg, Donald Gagné, Étienne Billard, Andrée-Anne Grosset, Nicolas Doucet, David Chatenet, Yves St-Pierre

Open access · diamondAbstract read
In one paragraph

Article in Oncotarget, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
1.1field-weighted citation impact, top 22% 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

17 citing papers in PubMed, 25 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Review
  7. Article
  8. Article
  9. Review
  10. Review
  11. Review
  12. Binding of a SolubleBiochemistry · 2020
    Article
  13. Article
  14. Article
  15. Galectin Targeted Therapy in Oncology: Current Knowledge and Perspectives.International journal of molecular sciences · 2018
    Review
  16. Galectin-7 in Epithelial Homeostasis and Carcinomas.International journal of molecular sciences · 2017
    Review
  17. 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

10 authors at 1 institution in 1 country.

Maria Claudia VladoiuINRS-Institut Armand-Frappier, Université du Québec, Laval, Québec, H7V 1B7 Canada.
Marilyne LabrieINRS-Institut Armand-Frappier, Université du Québec, Laval, Québec, H7V 1B7 Canada.
Myriam LétourneauINRS-Institut Armand-Frappier, Université du Québec, Laval, Québec, H7V 1B7 Canada.
Philippe EgesborgINRS-Institut Armand-Frappier, Université du Québec, Laval, Québec, H7V 1B7 Canada.
Donald GagnéINRS-Institut Armand-Frappier, Université du Québec, Laval, Québec, H7V 1B7 Canada.
Étienne BillardINRS-Institut Armand-Frappier, Université du Québec, Laval, Québec, H7V 1B7 Canada.
Andrée-Anne GrossetINRS-Institut Armand-Frappier, Université du Québec, Laval, Québec, H7V 1B7 Canada.
Nicolas DoucetINRS-Institut Armand-Frappier, Université du Québec, Laval, Québec, H7V 1B7 Canada.
David ChatenetINRS-Institut Armand-Frappier, Université du Québec, Laval, Québec, H7V 1B7 Canada.
Yves St-PierreINRS-Institut Armand-Frappier, Université du Québec, Laval, Québec, H7V 1B7 Canada.
Institut National de la Recherche Scientifique · CA

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Galectins are small soluble lectins that bind α-galactosides via their carbohydrate recognition domain (CRD). Their ability to dimerize is critical for the crosslinking of glycoprotein receptors and subsequent cellular signaling. This is particularly important in their immunomodulatory role via the induction of T-cell apoptosis. Because galectins play a central role in many pathologies, including cancer, they represent valuable therapeutic targets. At present, most inhibitors have been directed towards the CRD, a challenging task in terms of specificity given the high structural homology of the CRD among galectins. Such inhibitors are not effective at targeting CRD-independent functions of galectins. Here, we report a new class of galectin inhibitors that specifically binds human galectin-7 (hGal-7), disrupts the formation of homodimers, and inhibits the pro-apoptotic activity of hGal-7 on Jurkat T cells. In addition to representing a new means to achieve specificity when targeting galectins, such inhibitors provide a promising alternative to more conventional galectin inhibitors that target the CRD with soluble glycans or other small molecular weight allosteric inhibitors.

Indexed as

Drug DesignAmino Acid SequenceAmino Acid SubstitutionApoptosisBlotting, WesternGalectinsHumansJurkat CellsModels, MolecularPeptidesProtein BindingProtein MultimerizationProtein Structure, QuaternaryRecombinant ProteinsGalectinsLGALS7 protein, humanPeptidesRecombinant ProteinsapoptosisgalectininhibitorpeptideT-cells

Identifiers

PMID26543238
PMCPMC4747383
OpenAlexW2255004596

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.