Evidence map›Paper›PMID 24900426›Full record

ArticleACS medicinal chemistry letters2012

A new approach to explore the binding space of polysaccharide-based ligands: selectin antagonists.

Mickael Calosso, Daniel Charpentier, Marc Vaillancourt, Mohammed Bencheqroun, Gabrielle St-Pierre, Brian C Wilkes, Yvan Guindon

Open access · greenAbstract read
In one paragraph

Article in ACS medicinal chemistry letters, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing papers in PubMed
0.8field-weighted citation impact, top 32% 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

7 citing papers in PubMed, 19 citations in OpenAlex.

  1. Article
  2. Article
  3. Sialyl LewisACS medicinal chemistry letters · 2025
    Article
  4. Review
  5. Discovery ofJournal of medicinal chemistry · 2022
    Article
  6. Review
  7. 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.

Mickael CalossoBio-organic Chemistry and Chemical Biology and Peptide Research, Institut de recherches cliniques de Montréal (IRCM) , Montréal, Québec H2W 1R7, Canada.
Daniel CharpentierBio-organic Chemistry and Chemical Biology and Peptide Research, Institut de recherches cliniques de Montréal (IRCM) , Montréal, Québec H2W 1R7, Canada.
Marc VaillancourtBio-organic Chemistry and Chemical Biology and Peptide Research, Institut de recherches cliniques de Montréal (IRCM) , Montréal, Québec H2W 1R7, Canada.
Mohammed BencheqrounBio-organic Chemistry and Chemical Biology and Peptide Research, Institut de recherches cliniques de Montréal (IRCM) , Montréal, Québec H2W 1R7, Canada.
Gabrielle St-PierreBio-organic Chemistry and Chemical Biology and Peptide Research, Institut de recherches cliniques de Montréal (IRCM) , Montréal, Québec H2W 1R7, Canada.
Brian C WilkesBio-organic Chemistry and Chemical Biology and Peptide Research, Institut de recherches cliniques de Montréal (IRCM) , Montréal, Québec H2W 1R7, Canada.
Yvan GuindonBio-organic Chemistry and Chemical Biology and Peptide Research, Institut de recherches cliniques de Montréal (IRCM) , Montréal, Québec H2W 1R7, Canada ; Département de Chimie, Université de Montréal , C.P. 6128, succursale Centre-ville, Montréal, Québec H3C 3J7, Canada ; Department of Chemistry, McGill University , Montréal, Québec H3A 2K6, Canada.
McGill University · CA

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The discovery of molecules that interfere with the binding of a ligand to a receptor remains a topic of great interest in medicinal chemistry. Herein, we report that a monosaccharide unit of a polysaccharide ligand can be replaced advantageously by a conformationally locked acyclic molecular entity. A cyclic component of the selectin ligand Sialyl Lewis(x), GlcNAc, is replaced by an acyclic tether, tartaric esters, which link two saccharide units. The conformational bias of this acyclic tether originates from the minimization of intramolecular dipole-dipole interaction and the gauche effect. The evaluation of the binding of these derivatives to P-selectin was measured by surface plasmon resonance spectroscopy. The results obtained in our pilot study suggest that the discovery of tunable tethers could facilitate the exploration of the carbohydrate recognition domain of various receptors.

Indexed as

carbohydrate recognition domainpolysaccharide-based ligandsselectin antagonistsSialyl Lewisxsurface plasmon resonance spectroscopy

Identifiers

PMID24900426
PMCPMC4025734
OpenAlexW1983115893

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.