Evidence map›Paper›PMID 27563159›Full record

ArticleAngewandte Chemie (Weinheim an der Bergstrasse, Germany)2016

Compact, Polyvalent Mannose Quantum Dots as Sensitive, Ratiometric FRET Probes for Multivalent Protein-Ligand Interactions.

Yuan Guo, Chadamas Sakonsinsiri, Inga Nehlmeier, Martin A Fascione, Haiyan Zhang, Weili Wang, Stefan Pöhlmann, W Bruce Turnbull, Dejian Zhou

Open access · hybridAbstract read
In one paragraph

Article in Angewandte Chemie (Weinheim an der Bergstrasse, Germany), 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
1.6field-weighted citation impact, top 17% 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

3 citing papers in PubMed, 32 citations in OpenAlex.

  1. Article
  2. Visualization of Vaccine Dynamics with Quantum Dots for Immunotherapy.Angewandte Chemie (International ed. in English) · 2021
    Article
  3. 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

9 authors at 3 institutions in 2 countries.

Yuan GuoSchool of Chemistry and Astbury Centre for Structural Molecular Biology University of Leeds Leeds LS2 9JT UK.ORCID 0000-0003-4607-7356
Chadamas SakonsinsiriSchool of Chemistry and Astbury Centre for Structural Molecular Biology University of Leeds Leeds LS2 9JT UK.
Inga NehlmeierInfection Biology Unit German Primate Center Kellnerweg 4 37077 Göttingen Germany.
Martin A FascioneDepartment of Chemistry University of York Heslington York YO10 5DD UK.
Haiyan ZhangSchool of Chemistry and Astbury Centre for Structural Molecular Biology University of Leeds Leeds LS2 9JT UK.
Weili WangSchool of Chemistry and Astbury Centre for Structural Molecular Biology University of Leeds Leeds LS2 9JT UK.
Stefan PöhlmannInfection Biology Unit German Primate Center Kellnerweg 4 37077 Göttingen Germany.
W Bruce TurnbullSchool of Chemistry and Astbury Centre for Structural Molecular Biology University of Leeds Leeds LS2 9JT UK.ORCID 0000-0002-7352-0360
Dejian ZhouSchool of Chemistry and Astbury Centre for Structural Molecular Biology University of Leeds Leeds LS2 9JT UK.ORCID 0000-0003-3314-9242
University of Leeds · GBGerman Primate Center · DEUniversity of York · GB

Funding

Wellcome Trust
6 · The paper itself

Abstract

A highly efficient cap-exchange approach for preparing compact, dense polyvalent mannose-capped quantum dots (QDs) has been developed. The resulting QDs have been successfully used to probe multivalent interactions of HIV/Ebola receptors DC-SIGN and DC-SIGNR (collectively termed as DC-SIGN/R) using a sensitive, ratiometric Förster resonance energy transfer (FRET) assay. The QD probes specifically bind DC-SIGN, but not its closely related receptor DC-SIGNR, which is further confirmed by its specific blocking of DC-SIGN engagement with the Ebola virus glycoprotein. Tuning the QD surface mannose valency reveals that DC-SIGN binds more efficiently to densely packed mannosides. A FRET-based thermodynamic study reveals that the binding is enthalpy-driven. This work establishes QD FRET as a rapid, sensitive technique for probing structure and thermodynamics of multivalent protein-ligand interactions.

Indexed as

FRETKohlenhydrateProteineQuantenpunkteVirenhemmung

Identifiers

PMID27563159
PMCPMC4979676
OpenAlexW2302372370

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.