Evidence map›Paper›PMID 23780508›Full record

ArticleChemistry (Weinheim an der Bergstrasse, Germany)2013

The structural basis for optimal performance of oligothiophene-based fluorescent amyloid ligands: conformational flexibility is essential for spectral assignment of a diversity of protein aggregates.

Therése Klingstedt, Hamid Shirani, K O Andreas Åslund, Nigel J Cairns, Christina J Sigurdson, Michel Goedert, K Peter R Nilsson

Open access · greenAbstract read
In one paragraph

Article in Chemistry (Weinheim an der Bergstrasse, Germany), 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 65 papers.

0numbers the graph read from it
0cells of the map it votes in
65citing papers in PubMed
5.3field-weighted citation impact, top 4% 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

65 citing papers in PubMed, 116 citations in OpenAlex.

  1. A functional amyloid scaffold shapes insect egg coats.bioRxiv : the preprint server for biology · 2026
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  5. De novo design of protein binders to stabilize monomeric TDP-43 and inhibit its pathological aggregation.Proceedings of the National Academy of Sciences of the United States of America · 2025
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  17. Fluorescent optotracers for bacterial and biofilm detection and diagnostics.Science and technology of advanced materials · 2023
    Review
  18. Review
  19. Article
  20. Article

5 more citing papers are in PubMed but not listed here.

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 3 countries.

Therése KlingstedtDepartment of Chemistry, Linköping University, 581 83 Linköping, Sweden.
Hamid Shirani
K O Andreas Åslund
Nigel J Cairns
Christina J Sigurdson
Michel Goedert
K Peter R Nilsson
Linköping University · SEMRC Laboratory of Molecular Biology · GBUniversity of California San Diego · USWashington University in St. Louis · US

Funding

Smartphone-Based "Burst" Cognitive AssessmentsP01AG003991 · NIA · WASHINGTON UNIVERSITY · PI Tammie Lee Smith Benzinger · 1985 to 2026
$69.5M
WASHINGTON UNIVERSITY ALZHEIMERS DISEASE RESEARCH CENTERP50AG005681 · NIA · WASHINGTON UNIVERSITY · PI MORRIS, JOHN · 1985 to 2019
$52.1M
Mechanisms of Prion Aggregation and Species BarriersR01NS069566 · NINDS · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI ESKO, JEFFREY D, RAVITS, JOHN · 2011 to 2025
$5.7M
Mechanisms of Prion SpreadR01NS076896 · NINDS · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI SIGURDSON, CHRISTINA · 2012 to 2021
$3.4M
Medical Research Council MC_U105184291NIA NIH HHS 5P01-AG03991NIA NIH HHS P01 AG003991NIA NIH HHS P50 AG005681NIA NIH HHS P50AG05681NINDS NIH HHS R01 NS069566NINDS NIH HHS R01 NS076896Parkinson's UK K-1012
6 · The paper itself

Abstract

Protein misfolding diseases are characterized by deposition of protein aggregates, and optical ligands for molecular characterization of these disease-associated structures are important for understanding their potential role in the pathogenesis of the disease. Luminescent conjugated oligothiophenes (LCOs) have proven useful for optical identification of a broader subset of disease-associated protein aggregates than conventional ligands, such as thioflavin T and Congo red. Herein, the molecular requirements for achieving LCOs able to detect nonthioflavinophilic Aβ aggregates or non-congophilic prion aggregates, as well as spectrally discriminate Aβ and tau aggregates, were investigated. An anionic pentameric LCO was subjected to chemical engineering by: 1) replacing thiophene units with selenophene or phenylene moieties, or 2) alternating the anionic substituents along the thiophene backbone. In addition, two asymmetric tetrameric ligands were generated. Overall, the results from this study identified conformational freedom and extended conjugation of the conjugated backbone as crucial determinants for obtaining superior thiophene-based optical ligands for sensitive detection and spectral assignment of disease-associated protein aggregates.

Indexed as

Alzheimer DiseaseAmyloidAnimalsBrainFluorescent DyesMiceMice, TransgenicMolecular StructureProteinsStructure-Activity RelationshipThiophenesAmyloidFluorescent DyesProteinsThiophenesAlzheimer’s diseasefluorescent probesluminescent conjugated oligothiophenesmicroscopyprotein folding

Identifiers

PMID23780508
PMCPMC3884759
OpenAlexW2137028682

What OpenQuestion holds

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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.