Evidence map›Paper›PMID 21076980›Full record

ArticleMolecular diversity2011

Design, synthesis and activity evaluation of mannose-based DC-SIGN antagonists.

Nataša Obermajer, Sara Sattin, Cinzia Colombo, Michela Bruno, Urban Svajger, Marko Anderluh, Anna Bernardi

Open access · bronzeAbstract read
In one paragraph

Article in Molecular diversity, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing papers in PubMed
0.8field-weighted citation impact, top 29% 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

9 citing papers in PubMed, 32 citations in OpenAlex.

  1. Synthetic Ligands of Myeloid C-Type Lectin Receptors.Chembiochem : a European journal of chemical biology · 2026
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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 4 institutions in 2 countries.

Nataša ObermajerDepartment of Biotechnology, Jozef Stefan Institute, Jamova 39, 1000, Ljubljana, Slovenia.
Sara Sattin
Cinzia Colombo
Michela Bruno
Urban Svajger
Marko Anderluh
Anna Bernardi
University of Milan · ITBlood Transfusion Centre of Slovenia · SIJožef Stefan Institute · SIUniversity of Ljubljana · SI

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

In this article, we describe the design, synthesis and activity evaluation of glycomimetic DC-SIGN antagonists, that use a mannose residue to anchor to the protein carbohydrate recognition domain (CRD). The molecules were designed from the structure of the known pseudo-mannobioside antagonist 1, by including additional hydrophobic groups, which were expected to engage lipophilic areas of DC-SIGN CRD. The results demonstrate that the synthesized compounds potently inhibit DC-SIGN-mediated adhesion to mannan coated plates. Additionally, in silico docking studies were performed to rationalize the results and to suggest further optimization.

Indexed as

Drug DesignMannoseBiological AssayCell Adhesion MoleculesDC-Specific ICAM-3 Grabbing NonintegrinLectins, C-TypeModels, MolecularProtein BindingReceptors, Cell SurfaceReproducibility of ResultsStructure-Activity RelationshipCell Adhesion MoleculesDC-Specific ICAM-3 Grabbing NonintegrinLectins, C-TypeMannoseReceptors, Cell Surface

Identifiers

PMID21076980
PMCPMC7089406
OpenAlexW1973719870

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.