Evidence map›Paper›PMID 26013403›Full record

ArticleChemistry (Weinheim an der Bergstrasse, Germany)2015

Distinct Spacing Between Anionic Groups: An Essential Chemical Determinant for Achieving Thiophene-Based Ligands to Distinguish β-Amyloid or Tau Polymorphic Aggregates.

Therése Klingstedt, Hamid Shirani, Jasmin Mahler, Bettina M Wegenast-Braun, Sofie Nyström, Michel Goedert, Mathias Jucker, K Peter R Nilsson

Abstract read
In one paragraph

Article in Chemistry (Weinheim an der Bergstrasse, Germany), 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers, 2 of them syntheses that pooled it.

0numbers the graph read from it
0cells of the map it votes in
28citing papers in PubMed, 2 pooled it
–field-weighted citation impact
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

28 citing papers in PubMed, 2 syntheses or guidelines pooled it.

  1. Pooled it
  2. Impact of aging on animal models of Parkinson's disease.Frontiers in aging neuroscience · 2022
    Pooled it
  3. Article
  4. Review
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  14. Fluorescent optotracers for bacterial and biofilm detection and diagnostics.Science and technology of advanced materials · 2023
    Review
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  16. Article
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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

8 authors.

Therése KlingstedtDepartment of Chemistry, Linköping University, SE-581 83 Linköping (Sweden).
Hamid ShiraniDepartment of Chemistry, Linköping University, SE-581 83 Linköping (Sweden).
Jasmin MahlerDepartment of Cellular Neurology, Hertie Institute for Clinical Brain Research, University of Tübingen, Tübingen (Germany).
Bettina M Wegenast-BraunDepartment of Cellular Neurology, Hertie Institute for Clinical Brain Research, University of Tübingen, Tübingen (Germany).
Sofie NyströmDepartment of Chemistry, Linköping University, SE-581 83 Linköping (Sweden).
Michel GoedertMRC Laboratory of Molecular Biology, Cambridge (United Kingdom).
Mathias JuckerDepartment of Cellular Neurology, Hertie Institute for Clinical Brain Research, University of Tübingen, Tübingen (Germany).
K Peter R NilssonDepartment of Chemistry, Linköping University, SE-581 83 Linköping (Sweden). petni@ifm.liu.se.

Funding

Medical Research Council MC_U105184291
6 · The paper itself

Abstract

The accumulation of protein aggregates is associated with many devastating neurodegenerative diseases and the existence of distinct aggregated morphotypes has been suggested to explain the heterogeneous phenotype reported for these diseases. Thus, the development of molecular probes able to distinguish such morphotypes is essential. We report an anionic tetrameric oligothiophene compound that can be utilized for spectral assignment of different morphotypes of β-amyloid or tau aggregates present in transgenic mice at distinct ages. The ability of the ligand to spectrally distinguish between the aggregated morphotypes was reduced when the spacing between the anionic substituents along the conjugated thiophene backbone was altered, which verified that specific molecular interactions between the ligand and the protein aggregate are necessary to detect aggregate polymorphism. Our findings provide the structural and functional basis for the development of new fluorescent ligands that can distinguish between different morphotypes of protein aggregates.

Indexed as

Alzheimer DiseaseAmyloid beta-PeptidesAnimalsAnionsBrainFluorescent DyesHumansLigandsLuminescent AgentsMiceMolecular ProbesNeurodegenerative DiseasesProteinsThiophenesAmyloid beta-PeptidesAnionsFluorescent DyesLigandsLuminescent AgentsMolecular ProbesProteinsThiophenesaggregatesAlzheimer’s diseasefluorescenceluminescent conjugated oligothiophenesproteins

Identifiers

PMID26013403
PMCPMC4517144

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Registered trials

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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.