Evidence map›Paper›PMID 38109787›Full record

ArticleACS chemical neuroscience2024

EPR Studies of Aβ42 Oligomers Indicate a Parallel In-Register β-Sheet Structure.

Chelsea Jang, Diana Portugal Barron, Lan Duo, Christine Ma, Hanna Seabaugh, Zhefeng Guo

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in ACS chemical neuroscience, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing 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

2 citing papers in PubMed.

  1. Review
  2. 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.

Chelsea JangDepartment of Neurology, Brain Research Institute, David Geffen School of Medicine, University of California, Los Angeles, Los Angeles, California 90095, United States.
Diana Portugal BarronDepartment of Neurology, Brain Research Institute, David Geffen School of Medicine, University of California, Los Angeles, Los Angeles, California 90095, United States.ORCID 0009-0007-8737-9162
Lan DuoDepartment of Neurology, Brain Research Institute, David Geffen School of Medicine, University of California, Los Angeles, Los Angeles, California 90095, United States.
Christine MaDepartment of Neurology, Brain Research Institute, David Geffen School of Medicine, University of California, Los Angeles, Los Angeles, California 90095, United States.
Hanna SeabaughDepartment of Neurology, Brain Research Institute, David Geffen School of Medicine, University of California, Los Angeles, Los Angeles, California 90095, United States.
Zhefeng GuoDepartment of Neurology, Brain Research Institute, David Geffen School of Medicine, University of California, Los Angeles, Los Angeles, California 90095, United States.ORCID 0000-0003-1992-7255

Funding

Structural studies of amyloid beta globulomers with EPR spectroscopyR01AG050687 · NIA · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI GUO, ZHEFENG · 2017 to 2021
$1.9M
NIA NIH HHS R01 AG050687
6 · The paper itself

Abstract

Aβ aggregation leads to the formation of both insoluble amyloid fibrils and soluble oligomers. Understanding the structures of Aβ oligomers is important for delineating the mechanism of Aβ aggregation and developing effective therapeutics. Here, we use site-directed spin labeling and electron paramagnetic resonance (EPR) spectroscopy to study Aβ42 oligomers prepared by using the protocol of Aβ-derived diffusible ligands. We obtained the EPR spectra of 37 Aβ42 oligomer samples, each spin-labeled at a unique residue position of the Aβ42 sequence. Analysis of the disordered EPR components shows that the N-terminal region has a lower local structural stability. Spin label mobility analysis reveals three structured segments at residues 9-11, 15-22, and 30-40. Intermolecular spin-spin interactions indicate a parallel in-register β-sheet structure, with residues 34-38 forming the structural core. Residues 16-21 also adopt the parallel in-register β-structure, albeit with weaker intermolecular packing. Our results suggest that there is a structural class of Aβ oligomers that adopt fibril-like conformations.

Indexed as

Alzheimer DiseaseAmyloid beta-PeptidesAmyloidElectron Spin Resonance SpectroscopyHumansPeptide FragmentsProtein Conformation, beta-StrandSpin LabelsAmyloidAmyloid beta-PeptidesPeptide FragmentsSpin LabelsADDLsalzheimer’s diseaseamyloidelectron paramagnetic resonanceoligomersprotein aggregation

Identifiers

PMID38109787
PMCPMC10767747

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.