Evidence map›Paper›PMID 36645413›Full record

ArticleChemistry (Weinheim an der Bergstrasse, Germany)2023

Thiophene-Based Ligands for Histological Multiplex Spectral Detection of Distinct Protein Aggregates in Alzheimer's Disease.

Linda Lantz, Hamid Shirani, Bernardino Ghetti, Ruben Vidal, Therése Klingstedt, K Peter R Nilsson

Open access · hybridAbstract read
In one paragraph

Article in Chemistry (Weinheim an der Bergstrasse, Germany), 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing 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

5 citing papers in PubMed, 12 citations in OpenAlex.

  1. Review
  2. Article
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  5. Review
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

6 authors at 2 institutions in 2 countries.

Linda LantzDepartment of Physics, Chemistry and Biology, Linköping University, 581 83, Linköping, Sweden.
Hamid ShiraniDepartment of Physics, Chemistry and Biology, Linköping University, 581 83, Linköping, Sweden.
Bernardino GhettiDepartment of Pathology and Laboratory Medicine, Indiana University School of Medicine, Indianapolis, 46202, Indiana, USA.
Ruben VidalDepartment of Pathology and Laboratory Medicine, Indiana University School of Medicine, Indianapolis, 46202, Indiana, USA.
Therése KlingstedtDepartment of Physics, Chemistry and Biology, Linköping University, 581 83, Linköping, Sweden.
K Peter R NilssonDepartment of Physics, Chemistry and Biology, Linköping University, 581 83, Linköping, Sweden.ORCID http://orcid.org/0000-0002-5582-140X
Linköping University · SEIndiana University School of Medicine

Funding

Atomic models of human tau filaments and development of tau ligandsU01NS110437 · NINDS · INDIANA UNIVERSITY INDIANAPOLIS · PI GHETTI, BERNARDINO FRANCESCO, JIANG, WEN · 2018 to 2022
$3.5M
AlzheimerfondenFoundation for the National Institutes of Health U01NS110437HjärnfondenKonung Gustaf V:s och Drottning Victorias FrimurarestiftelseNINDS NIH HHS U01 NS110437Torsten Söderbergs StiftelseVetenskapsrådet 2016-00748
6 · The paper itself

Abstract

The aggregation and accumulation of proteins in the brain is the defining feature of many devastating neurodegenerative diseases. The development of fluorescent ligands that bind to these accumulations, or deposits, is essential for the characterization of these neuropathological lesions. We report the synthesis of donor-acceptor-donor (D-A-D) thiophene-based ligands with different emission properties. The D-A-D ligands displayed selectivity towards distinct disease-associated protein deposits in histological sections from postmortem brain tissue of individuals affected by Alzheimer's disease (AD). The ability of the ligands to selectively identify AD-associated pathological alterations, such as deposits composed of aggregates of the amyloid-β (Aβ) peptide or tau, was reduced when the chemical composition of the ligands was altered. When combining the D-A-D ligands with conventional thiophene-based ligands, superior spectral separation of distinct protein aggregates in AD tissue sections was obtained. Our findings provide the structural and functional basis for the development of new fluorescent ligands that can distinguish between aggregated proteinaceous species, as well as offer novel strategies for developing multiplex fluorescence detection of protein aggregates in tissue sections.

Indexed as

Alzheimer DiseaseAmyloid beta-PeptidesBrainHumansLigandsProtein Aggregatestau ProteinsThiophenesAmyloid beta-PeptidesLigandsProtein Aggregatestau ProteinsThiophenesAlzheimer's diseaseamyloid-βfluorescent ligandsprotein aggregatestau

Identifiers

PMID36645413
PMCPMC10101888
OpenAlexW4316674134

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.