Evidence map›Paper›PMID 34590866›Full record

ArticleThe journal of physical chemistry letters2021

Label-Free Infrared Spectroscopic Imaging Reveals Heterogeneity of β-Sheet Aggregates in Alzheimer's Disease.

Matthew P Confer, Brooke M Holcombe, Abigail G Foes, John M Holmquist, Savannah C Walker, Sanghamitra Deb, Ayanjeet Ghosh

Abstract read
In one paragraph

Article in The journal of physical chemistry letters, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
–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

12 citing papers in PubMed.

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  12. Recent update on the heterogeneity of the Alzheimer's disease spectrum.Journal of neural transmission (Vienna, Austria : 1996) · 2022
    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

7 authors.

Matthew P ConferDepartment of Chemistry and Biochemistry, University of Alabama, Tuscaloosa AL-35401, United States.ORCID https://orcid.org/0000-0002-0856-3583
Brooke M HolcombeDepartment of Chemistry and Biochemistry, University of Alabama, Tuscaloosa AL-35401, United States.
Abigail G FoesDepartment of Chemistry and Biochemistry, University of Alabama, Tuscaloosa AL-35401, United States.
John M HolmquistDepartment of Chemistry and Biochemistry, University of Alabama, Tuscaloosa AL-35401, United States.
Savannah C WalkerDepartment of Chemistry and Biochemistry, University of Alabama, Tuscaloosa AL-35401, United States.
Sanghamitra DebDepartment of Chemistry and Biochemistry, University of Alabama, Tuscaloosa AL-35401, United States.
Ayanjeet GhoshDepartment of Chemistry and Biochemistry, University of Alabama, Tuscaloosa AL-35401, United States.ORCID https://orcid.org/0000-0001-9458-3910

Funding

Investigating structural heterogeneities in amyloid aggregates with multiscale infrared spectroscopic imagingR35GM138162 · NIGMS · UNIVERSITY OF ALABAMA IN TUSCALOOSA · PI GHOSH, AYANJEET · 2020 to 2024
$2.0M
NIGMS NIH HHS R35 GM138162
6 · The paper itself

Abstract

The aggregation of the amyloid beta (Aβ) protein into plaques is a pathological feature of Alzheimer's disease (AD). While amyloid aggregates have been extensively studied in vitro, their structural aspects and associated chemistry in the brain are not fully understood. In this report, we demonstrate, using infrared spectroscopic imaging, that Aβ plaques exhibit significant heterogeneities in terms of their secondary structure and phospholipid content. We show that the capabilities of discrete frequency infrared imaging (DFIR) are ideally suited for characterization of amyloid deposits in brain tissues and employ DFIR to identify nonplaque β-sheet aggregates distributed throughout brain tissues. We further demonstrate that phospholipid-rich β-sheet deposits exist outside of plaques in all diseased tissues, indicating their potential clinical significance. This is the very first application of DFIR toward a characterization of protein aggregates in an AD brain and provides a rapid, label-free approach that allows us to uncover β-sheet heterogeneities in the AD, which may be significant for targeted therapeutic strategies in the future.

Indexed as

Spectrophotometry, InfraredAlzheimer DiseaseAmyloid beta-PeptidesBrainHumansProtein AggregatesProtein Conformation, beta-StrandAmyloid beta-PeptidesProtein Aggregates

Identifiers

PMID34590866
PMCPMC8933041

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.