Evidence map›Paper›PMID 34156433›Full record

ReviewBiochemical Society transactions2021

Utilizing magnetic resonance techniques to study membrane interactions of amyloid peptides.

Sunnia Rajput, Marc-Antoine Sani, David W Keizer, Frances Separovic

Open access · hybridAbstract readReview
PubMed Full text at PMC Publisher
In one paragraph

Review in Biochemical Society transactions, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
0.7field-weighted citation impact, top 31% 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

3 citing papers in PubMed, 8 citations in OpenAlex.

  1. Article
  2. Article
  3. In-cellBiophysical chemistry · 2023
    Article
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

4 authors at 1 institution in 1 country.

Sunnia RajputBio21 Molecular Science & Biotechnology Institute, University of Melbourne, Melbourne, VIC 3010, Australia.ORCID 0000-0003-3068-4098
Marc-Antoine SaniBio21 Molecular Science & Biotechnology Institute, University of Melbourne, Melbourne, VIC 3010, Australia.ORCID 0000-0003-3284-2176
David W KeizerBio21 Molecular Science & Biotechnology Institute, University of Melbourne, Melbourne, VIC 3010, Australia.ORCID 0000-0002-0442-0999
Frances SeparovicBio21 Molecular Science & Biotechnology Institute, University of Melbourne, Melbourne, VIC 3010, Australia.ORCID 0000-0002-6484-2763
The University of Melbourne · AU

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Alzheimer's disease (AD) is a common neurodegenerative condition that involves the extracellular accumulation of amyloid plaques predominantly consisting of Aβ peptide aggregates. The amyloid plaques and soluble oligomeric species of Aβ are believed to be the major cause of synaptic dysfunction in AD brain and their cytotoxic mechanisms have been proposed to involve interactions with cell membranes. In this review, we discuss our solid-state nuclear magnetic resonance (ssNMR) studies of Aβ interactions with model membranes.

Indexed as

Alzheimer DiseaseAmyloidAmyloid beta-PeptidesAmyloid beta-Protein PrecursorBrainCell MembraneHumansMagnetic Resonance SpectroscopyNeuronsPlaque, AmyloidProtein BindingSynapsesAmyloidAmyloid beta-PeptidesAmyloid beta-Protein PrecursorAlzheimers diseaseamyloid betamembranesNMR spectroscopyphospholipids

Identifiers

PMID34156433
PMCPMC8286822
OpenAlexW3175388523

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.