Evidence map›Paper›PMID 25495506›Full record

ArticlePrion2014

Multimodal fluorescence microscopy of prion strain specific PrP deposits stained by thiophene-based amyloid ligands.

Karin Magnusson, Rozalyn Simon, Daniel Sjölander, Christina J Sigurdson, Per Hammarström, K Peter R Nilsson

Open access · hybridAbstract read
In one paragraph

Article in Prion, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 45 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
45citing papers in PubMed, 1 pooled it
3.1field-weighted citation impact, top 8% 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

45 citing papers in PubMed, 1 synthesis or guideline pooled it, 72 citations in OpenAlex.

  1. Pooled it
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  12. EMBER multidimensional spectral microscopy enables quantitative determination of disease- and cell-specific amyloid strains.Proceedings of the National Academy of Sciences of the United States of America · 2023
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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

6 authors at 2 institutions in 2 countries.

Karin Magnussona Department of Chemistry ; Linköping University ; Linköping , Sweden.
Rozalyn Simon
Daniel Sjölander
Christina J Sigurdson
Per Hammarström
K Peter R Nilsson
Linköping University · SEUniversity of California, San Diego · US

Funding

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
NINDS NIH HHS R01 NS069566NINDS NIH HHS R01 NS076896
6 · The paper itself

Abstract

The disease-associated prion protein (PrP) forms aggregates which vary in structural conformation yet share an identical primary sequence. These variations in PrP conformation are believed to manifest in prion strains exhibiting distinctly different periods of disease incubation as well as regionally specific aggregate deposition within the brain. The anionic luminescent conjugated polythiophene (LCP), polythiophene acetic acid (PTAA) has previously been used to distinguish PrP deposits associated with distinct mouse adapted strains via distinct fluorescence emission profiles from the dye. Here, we employed PTAA and 3 structurally related chemically defined luminescent conjugated oligothiophenes (LCOs) to stain brain tissue sections from mice inoculated with 2 distinct prion strains. Our results showed that in addition to emission spectra, excitation, and fluorescence lifetime imaging microscopy (FLIM) can fruitfully be assessed for optical distinction of PrP deposits associated with distinct prion strains. Our findings support the theory that alterations in LCP/LCO fluorescence are due to distinct conformational restriction of the thiophene backbone upon interaction with PrP aggregates associated with distinct prion strains. We foresee that LCP and LCO staining in combination with multimodal fluorescence microscopy might aid in detecting structural differences among discrete protein aggregates and in linking protein conformational features with disease phenotypes for a variety of neurodegenerative proteinopathies.

Indexed as

AnimalsBrainFluorescent DyesLigandsMiceMicroscopy, FluorescenceOptical ImagingPolymersPrion DiseasesPrionsProtein AggregatesProtein Aggregation, PathologicalThiophenesFluorescent DyesLigandsPolymerspolythiophenePrionsProtein AggregatesThiophenesAD, Alzheimer disease; LCOs, luminescent conjugated oligothiophenes; LCPs, luminescent conjugated polythiophenes; mSS, murine sheep scrapie; mCWD, murine chronic wasting disease; PrP, prion proteinamyloidfluorescent probesimagingluminescent conjugated polythiophenesmicroscopyprion strainprotein aggregates

Identifiers

PMID25495506
PMCPMC4601348
OpenAlexW1989173606

What OpenQuestion holds

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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.