Evidence map›Paper›PMID 22639721›Full record

ArticleChemical science2012

Quinoxalinone Inhibitors of the Lectin DC-SIGN.

Shane L Mangold, Lynne R Prost, Laura L Kiessling

Open access · greenAbstract read
In one paragraph

Article in Chemical science, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
2.1field-weighted citation impact, top 13% 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

19 citing papers in PubMed, 79 citations in OpenAlex.

  1. Synthetic Ligands of Myeloid C-Type Lectin Receptors.Chembiochem : a European journal of chemical biology · 2026
    Review
  2. Article
  3. Article
  4. Secondary Sites of the C-type Lectin-Like Fold.Chemistry (Weinheim an der Bergstrasse, Germany) · 2024
    Review
  5. Review
  6. Article
  7. Review
  8. Article
  9. Article
  10. Review
  11. Review
  12. Review
  13. Article
  14. Article
  15. Article
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  17. Article
  18. Glycopolymer probes of signal transduction.Chemical Society reviews · 2013
    Review
  19. 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

3 authors at 1 institution in 1 country.

Shane L MangoldDepartment of Chemistry, University of Wisconsin-Madison, Madison, WI, 53706, USA.
Lynne R Prost
Laura L Kiessling
University of Wisconsin–Madison · US

Funding

PROBES OF CARBOHYDRATE FUNCTIONR01GM049975 · NIGMS · UNIVERSITY OF WISCONSIN-MADISON · PI KIESSLING, LAURA L · 1999 to 2016
$5.2M
Probing Function of the C-type Lectin DC-SIGN with Glycomimetic LigandsF32GM089084 · NIGMS · UNIVERSITY OF WISCONSIN-MADISON · PI PROST, LYNNE · 2010 to 2011
$92k
BIOORGANIC STUDIES OF CARBOHYDRATE FUNCTIONR29GM049975 · NIGMS · UNIVERSITY OF WISCONSIN MADISON · PI KIESSLING, LAURA L · 1993 to 1997
–
PURCHASE OF A 1409 TESLA NMR INSTRUMENTS10RR013866 · NCRR · UNIVERSITY OF WISCONSIN MADISON · PI GELLMAN, SAMUEL H. · 1999 to 1999
–
NCRR NIH HHS S10 RR013866NIGMS NIH HHS F32 GM089084NIGMS NIH HHS R01 GM049975NIGMS NIH HHS R29 GM049975
6 · The paper itself

Abstract

The C-type lectin dendritic cell-specific intercellular adhesion molecule 3-grabbing nonintegrin (DC-SIGN) can serve as a docking site for pathogens on the surface of dendritic cells. Pathogen binding to DC-SIGN can have diverse consequences for the host. DC-SIGN can facilitate HIV-1 dissemination, but the interaction of Mycobacterium tuberculosis with DC-SIGN is important for host immunity. The ability of pathogens to target DC-SIGN provides impetus to identify ligands that can perturb these interactions. Here, we describe the first stable small molecule inhibitors of DC-SIGN. These inhibitors were derived from a collection of quinoxalinones, which were assembled using a tandem cross metathesis-hydrogenation sequence. To assess the ability of these small molecules to block DC-SIGN-mediated glycan adhesion and internalization, we developed a sensitive flow cytometry assay. Our results reveal that the quinoxalinones are effective inhibitors of DC-SIGN-glycan interactions. These compounds block both glycan binding to cells and glycan internalization. We anticipate that these non-carbohydrate inhibitors can be used to elucidate the role of DC-SIGN in pathogenesis and immune function.

Identifiers

PMID22639721
PMCPMC3359018
OpenAlexW2041778517

What OpenQuestion holds

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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.