Evidence map›Paper›PMID 32300761›Full record

ReviewChemical communications (Cambridge, England)2020

High-resolution probing of early events in amyloid-β aggregation related to Alzheimer's disease.

Bikash R Sahoo, Sarah J Cox, Ayyalusamy Ramamoorthy

Open access · greenAbstract readReview
In one paragraph

Review in Chemical communications (Cambridge, England), 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.

0numbers the graph read from it
0cells of the map it votes in
34citing papers in PubMed
8.3field-weighted citation impact, top 2% 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

34 citing papers in PubMed, 84 citations in OpenAlex.

  1. Review
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  8. Review
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  12. Ganglioside GM1 produces stable, short, and cytotoxic AβChemical communications (Cambridge, England) · 2023
    Article
  13. Review
  14. Article
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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

3 authors at 1 institution in 1 country.

Bikash R SahooBiophysics Program, Department of Chemistry, University of Michigan, Ann Arbor, MI 48109-1055, USA. ramamoor@umich.edu.
Sarah J Cox
Ayyalusamy Ramamoorthy
University of Michigan · US

Funding

Membrane interaction and disruption by the Alzheimer's amyloid-beta peptideR01AG048934 · NIA · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI RAMAMOORTHY, AYYALUSAMY · 2016 to 2020
$2.0M
NIA NIH HHS R01 AG048934
6 · The paper itself

Abstract

In Alzheimer's disease (AD), soluble oligomers of amyloid-β (Aβ) are emerging as a crucial entity in driving disease progression as compared to insoluble amyloid deposits. The lacuna in establishing the structure to function relationship for Aβ oligomers prevents the development of an effective treatment for AD. While the transient and heterogeneous properties of Aβ oligomers impose many challenges for structural investigation, an effective use of a combination of NMR techniques has successfully identified and characterized them at atomic-resolution. Here, we review the successful utilization of solution and solid-state NMR techniques to probe the aggregation and structures of small and large oligomers of Aβ. Biophysical studies utilizing the commonly used solution and

Indexed as

Protein Aggregation, PathologicalAlzheimer DiseaseAmyloid beta-PeptidesNuclear Magnetic Resonance, BiomolecularAmyloid beta-Peptides

Identifiers

PMID32300761
PMCPMC7254607
OpenAlexW3015200124

What OpenQuestion holds

Textmetadata
LicenceTDM
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.