Evidence map›Paper›PMID 32195099›Full record

ArticleAdvanced science (Weinheim, Baden-Wurttemberg, Germany)2020

Super-Resolution Infrared Imaging of Polymorphic Amyloid Aggregates Directly in Neurons.

Oxana Klementieva, Christophe Sandt, Isak Martinsson, Mustafa Kansiz, Gunnar K Gouras, Ferenc Borondics

Open access · goldAbstract read
In one paragraph

Article in Advanced science (Weinheim, Baden-Wurttemberg, Germany), 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 53 papers.

0numbers the graph read from it
0cells of the map it votes in
53citing papers in PubMed
9.2field-weighted citation impact, top 1% 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

53 citing papers in PubMed, 122 citations in OpenAlex.

  1. Article
  2. From Disordered to Ordered: Nanoscale Spectroscopy Reveals Structural Evolution of Amyloid Beta 40 Fibrils.Chemphyschem : a European journal of chemical physics and physical chemistry · 2026
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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 3 institutions in 3 countries.

Oxana KlementievaMedical Microspectroscopy Research Group Department of Experimental Medical Science Lund University 22180 Lund Sweden.ORCID https://orcid.org/0000-0003-1782-050X
Christophe SandtSynchrotron SOLEIL L'Orme des Merisiers 91192 Gif Sur Yvette Cedex France.
Isak MartinssonExperimental Dementia Research Department of Experimental Medical Science Lund University 22180 Lund Sweden.
Mustafa KansizPhotothermal Spectroscopy Corporation Santa Barbara CA 93101 USA.
Gunnar K GourasExperimental Dementia Research Department of Experimental Medical Science Lund University 22180 Lund Sweden.
Ferenc BorondicsSynchrotron SOLEIL L'Orme des Merisiers 91192 Gif Sur Yvette Cedex France.
Lund University · SESynchrotron soleil · FRSpectros Corporation (United States) · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Loss of memory during Alzheimer's disease (AD), a fatal neurodegenerative disorder, is associated with neuronal loss and the aggregation of amyloid proteins into neurotoxic β-sheet enriched structures. However, the mechanism of amyloid protein aggregation is still not well understood due to many challenges when studying the endogenous amyloid structures in neurons or in brain tissue. Available methods either require chemical processing of the sample or may affect the amyloid protein structure itself. Therefore, new approaches, which allow studying molecular structures directly in neurons, are urgently needed. A novel approach is tested, based on label-free optical photothermal infrared super-resolution microspectroscopy, to study AD-related amyloid protein aggregation directly in the neuron at sub-micrometer resolution. Using this approach, amyloid protein aggregates are detected at the subcellular level, along the neurites and strikingly, in dendritic spines, which has not been possible until now. Here, a polymorphic nature of amyloid structures that exist in AD transgenic neurons is reported. Based on the findings of this work, it is suggested that structural polymorphism of amyloid proteins that occur already in neurons may trigger different mechanisms of AD progression.

Indexed as

Alzheimer's diseasedisease mechanismoptical photothermal infrared spectroscopyprotein aggregationstructure–function relationsuper‐resolution

Identifiers

PMID32195099
PMCPMC7080554
OpenAlexW3004475249

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.