Evidence map›Paper›PMID 35129859›Full record

ArticleProtein science : a publication of the Protein Society2022

Molecular insights into the primary nucleation of polymorphic amyloid β dimers in DOPC lipid bilayer membrane.

Olga Press-Sandler, Yifat Miller

Open access · hybridAbstract read
In one paragraph

Article in Protein science : a publication of the Protein Society, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
2.6field-weighted citation impact, top 9% 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

11 citing papers in PubMed, 24 citations in OpenAlex.

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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

2 authors at 1 institution in 1 country.

Olga Press-SandlerDepartment of Chemistry, Ben-Gurion University of the Negev, Be'er Sheva, Israel.
Yifat MillerDepartment of Chemistry, Ben-Gurion University of the Negev, Be'er Sheva, Israel.ORCID 0000-0002-1163-9745
Ben-Gurion University of the Negev · IL

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Alzheimer's disease (AD) pathology is characterized by loss of memory cognitive and behavioral deterioration. One of the hallmarks of AD is amyloid β (Aβ) plaques in the brain that consists of Aβ oligomers and fibrils. It is accepted that oligomers, particularly dimers, are toxic species that are produced extracellularly and intracellularly in membranes. It is believed that the disruption of membranes by polymorphic Aβ oligomers is the key for the pathology of AD. This is a first study that investigate the effect of polymorphic "α-helix/random coil" and "fibril-like" Aβ dimers on 1,2-dioleoyl-sn-glycero-3-phosphocholine (DOPC) membrane. It has been found that the DOPC membrane promotes Aβ

Indexed as

Alzheimer DiseaseLipid BilayersAmyloidAmyloid beta-PeptidesHumansPeptide FragmentsPhosphatidylcholines1,2-oleoylphosphatidylcholineAmyloidAmyloid beta-PeptidesLipid BilayersPeptide FragmentsPhosphatidylcholinesAlzheimer's diseaseamyloidsDOPC membraneneurodegenerative diseaseprotein aggregation

Identifiers

PMID35129859
PMCPMC8994488
OpenAlexW4210834259

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.